Gerd Krause

Summary

Country: Germany

Publications

  1. pmc Comparative sequence and structural analyses of G-protein-coupled receptor crystal structures and implications for molecular models
    Catherine L Worth
    Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
    PLoS ONE 4:e7011. 2009
  2. pmc Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    PLoS ONE 5:e9745. 2010
  3. pmc Molecular sampling of the allosteric binding pocket of the TSH receptor provides discriminative pharmacophores for antagonist and agonists
    Inna Hoyer
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    Biochem Soc Trans 41:213-7. 2013
  4. pmc Primary and secondary thyroid hormone transporters
    Anita Kinne
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Roessle Str, 10, 13125 Berlin, Germany
    Thyroid Res 4:S7. 2011
  5. pmc From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs)
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    J Biol Chem 286:25859-71. 2011
  6. doi Structure and function of extracellular claudin domains
    Gerd Krause
    Leibniz Institut fuer Molekulare Pharmakologie, Berlin, Germany
    Ann N Y Acad Sci 1165:34-43. 2009
  7. pmc Defining structural and functional dimensions of the extracellular thyrotropin receptor region
    Gunnar Kleinau
    Department for Structural Biology, Leibniz Institut fur Molekulare Pharmakologie, D 13125 Berlin, Germany
    J Biol Chem 286:22622-31. 2011
  8. pmc Evidence for cooperative signal triggering at the extracellular loops of the TSH receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, D 13125 Berlin, Germany
    FASEB J 22:2798-808. 2008
  9. pmc Signaling-sensitive amino acids surround the allosteric ligand binding site of the thyrotropin receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, D 13125 Berlin, Germany
    FASEB J 24:2347-54. 2010
  10. ncbi The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding
    Anja Thielen
    Forschungsinstitut für Molekulare Pharmakologie FMP, Robert Rossle Str 10, 13125 Berlin, Germany
    FEBS Lett 579:5227-35. 2005

Collaborators

Detail Information

Publications44

  1. pmc Comparative sequence and structural analyses of G-protein-coupled receptor crystal structures and implications for molecular models
    Catherine L Worth
    Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
    PLoS ONE 4:e7011. 2009
    ..The aim of this study is therefore to perform a systematic and detailed analysis of sequence-structure relationships of known GPCR structures...
  2. pmc Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    PLoS ONE 5:e9745. 2010
    ....
  3. pmc Molecular sampling of the allosteric binding pocket of the TSH receptor provides discriminative pharmacophores for antagonist and agonists
    Inna Hoyer
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    Biochem Soc Trans 41:213-7. 2013
    ..It prepares the basis for rational optimization of new high-affinity antagonists to interfere with the pathogenic activation of the TSHR...
  4. pmc Primary and secondary thyroid hormone transporters
    Anita Kinne
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Roessle Str, 10, 13125 Berlin, Germany
    Thyroid Res 4:S7. 2011
    ..Thereby, we focus on TH transporters occurring in the blood-brain barrier...
  5. pmc From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs)
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    J Biol Chem 286:25859-71. 2011
    ..Our findings might be relevant for all family A GPCRs as supported by a statistical analysis of residue properties between the TMHs of a vast number of GPCR sequences...
  6. doi Structure and function of extracellular claudin domains
    Gerd Krause
    Leibniz Institut fuer Molekulare Pharmakologie, Berlin, Germany
    Ann N Y Acad Sci 1165:34-43. 2009
    ..These considerations may reveal the ECLs of claudins as decisive submolecular determinants that specify the function of a claudin...
  7. pmc Defining structural and functional dimensions of the extracellular thyrotropin receptor region
    Gunnar Kleinau
    Department for Structural Biology, Leibniz Institut fur Molekulare Pharmakologie, D 13125 Berlin, Germany
    J Biol Chem 286:22622-31. 2011
    ....
  8. pmc Evidence for cooperative signal triggering at the extracellular loops of the TSH receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, D 13125 Berlin, Germany
    FASEB J 22:2798-808. 2008
    ..Our findings provide new insights concerning molecular signal transmission from extracellular domains toward the transmembrane helix bundle of the glycoprotein hormone receptors...
  9. pmc Signaling-sensitive amino acids surround the allosteric ligand binding site of the thyrotropin receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, D 13125 Berlin, Germany
    FASEB J 24:2347-54. 2010
    ..Our findings of signaling-sensitive residues in this region of the transmembrane bundle may be of general importance as this domain appears to be evolutionarily retained among GPCRs...
  10. ncbi The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding
    Anja Thielen
    Forschungsinstitut für Molekulare Pharmakologie FMP, Robert Rossle Str 10, 13125 Berlin, Germany
    FEBS Lett 579:5227-35. 2005
    ..Instead, they are necessary to establish a transport-competent folding state in the early secretory pathway...
  11. pmc Mutations that silence constitutive signaling activity in the allosteric ligand-binding site of the thyrotropin receptor
    Ann Karin Haas
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125, Berlin, Germany
    Cell Mol Life Sci 68:159-67. 2011
    ..We suggest that the amino acid positions identified herein are indicating locations where small-molecule antagonists, both neutral antagonists and inverse agonists, might interfere with active TSHR conformations...
  12. ncbi Differences between lutropin-mediated and choriogonadotropin-mediated receptor activation
    Paul Grzesik
    Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
    FEBS J 281:1479-92. 2014
    ....
  13. ncbi Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Rossle Str 10, D 13125 Berlin, Germany
    J Biol Chem 282:518-25. 2007
    ..These and other mutant phenotypes reported here support a dynamic interface between TMH6 and ECL2. Disruption of this critical interface for signaling by introduction of mutations in TSHR can either increase or decrease basal activity...
  14. doi Structural determinants for selective recognition of peptide ligands for endothelin receptor subtypes ETA and ETB
    Jens Lättig
    Leibniz Insitut für Molekulare Pharmakologie FMP, 13125 Berlin, Germany
    J Pept Sci 15:479-91. 2009
    ..A narrow tunnel shape in ET(A) is restrictive for a selected group of peptide ligands' N-termini, whereas a broad funnel-shaped entrance in ET(B) accepts a variety of different shapes and properties of ligands...
  15. ncbi Formation of tight junction: determinants of homophilic interaction between classic claudins
    Jörg Piontek
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    FASEB J 22:146-58. 2008
    ..Since nearly all these residues are conserved in most claudins, our findings are of general relevance for all classical claudins. On the basis of the data we have established a novel molecular concept for tight junction formation...
  16. pmc Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3
    Lars Winkler
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rössle Strasse, 10, 13125 Berlin, Germany
    J Biol Chem 284:18863-72. 2009
    ..The data can be used for the specific design of CPE-based modulators of tight junctions, to improve drug delivery, and as chemotherapeutics for tumors overexpressing claudins...
  17. pmc Claudin-3 and claudin-5 protein folding and assembly into the tight junction are controlled by non-conserved residues in the transmembrane 3 (TM3) and extracellular loop 2 (ECL2) segments
    Jan Rossa
    From the Leibniz Institut für Molekulare Pharmakologie, Department of Structural Biology, 13125 Berlin, Germany
    J Biol Chem 289:7641-53. 2014
    ....
  18. pmc Mechanism of Clostridium perfringens enterotoxin interaction with claudin-3/-4 protein suggests structural modifications of the toxin to target specific claudins
    Anna Veshnyakova
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
    J Biol Chem 287:1698-708. 2012
    ..The obtained mutants and mechanistic insights will advance the design of cCPE-based modulators to target specific claudin subtypes related either to paracellular barriers that impede drug delivery or to tumors...
  19. ncbi Structure and function of claudins
    Gerd Krause
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    Biochim Biophys Acta 1778:631-45. 2008
    ..The concepts evolved from these findings and first tentative molecular models for homophilic interactions may explain the different functional contribution of the two extracellular loops at tight junctions...
  20. pmc High-affinity AKAP7delta-protein kinase A interaction yields novel protein kinase A-anchoring disruptor peptides
    Christian Hundsrucker
    Leibniz Institut fur Molekulare Pharmakologie, Campus Berlin Buch, Robert Rossle Str 10, 13125 Berlin, Germany
    Biochem J 396:297-306. 2006
    ....
  21. ncbi An interactive web-tool for molecular analyses links naturally occurring mutation data with three-dimensional structures of the rhodopsin-like glycoprotein hormone receptors
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie FMP, D 13125 Berlin, Germany
    Hum Mutat 31:E1519-25. 2010
    ..Our new application has been incorporated into a freely available database and website for the GPHRs (http://www.ssfa-gphr.de), but the principle development would also be applicable to other macromolecules...
  22. doi Domain Interaction Footprint: a multi-classification approach to predict domain-peptide interactions
    Christian Schillinger
    Leibniz Institute for Molecular Pharmacology, Robert Roessle Strasse 10, Berlin, FU Berlin, Germany
    Bioinformatics 25:1632-9. 2009
    ..Second, we show that our method is able to create a multi-classification model that assesses the binding specificity of a given peptide to all examined PRMs at once...
  23. ncbi Quantification of PDZ domain specificity, prediction of ligand affinity and rational design of super-binding peptides
    Urs Wiedemann
    Forschungsinstitut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    J Mol Biol 343:703-18. 2004
    ..This approach allows the rational design of functional experiments and provides a basis for simulating interaction networks in the field of systems biology...
  24. ncbi Discovery of low-molecular-weight ligands for the AF6 PDZ domain
    Mangesh Joshi
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Roessle Strasse 10, 13125 Berlin, Germany
    Angew Chem Int Ed Engl 45:3790-5. 2006
  25. ncbi Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, D 13125 Berlin, Germany
    Mol Endocrinol 21:574-80. 2007
    ..Moreover, new interrelations of determinants important for selective G protein-mediated activation of GPHRs are resumed...
  26. doi A heterozygous mutation in the third transmembrane domain causes a dominant-negative effect on signalling capability of the MC4R
    Patrick Tarnow
    Department of Pediatric Endocrinology, Charite, Campus Virchow Klinikum Universitatsmedizin Berlin, Berlin, Germany
    Obes Facts 1:155-62. 2008
    ..For most MC4R mutations a gene dosage effect seems to be the underlying mechanism. However, a dominant negative effect of a heterozygous MC4R mutation was recently identified, pointing to an additional mechanism of MC4R inactivation...
  27. doi Discovery, structure-activity relationship studies, and crystal structure of nonpeptide inhibitors bound to the Shank3 PDZ domain
    Jörn Saupe
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Rossle Str 10, 13125 Berlin, Germany
    ChemMedChem 6:1411-22. 2011
    ..The structure, analyzed at a resolution of 1.85 Å, reveals details of the binding mode. Finally, binding to PDZ domains of PSD-95, syntrophin, and DVL3 was studied using ¹H,¹⁵N HSQC NMR spectroscopy...
  28. doi Research resource: novel structural insights bridge gaps in glycoprotein hormone receptor analyses
    Annika Kreuchwig
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    Mol Endocrinol 27:1357-63. 2013
    ....
  29. doi Thyrotropin and homologous glycoprotein hormone receptors: structural and functional aspects of extracellular signaling mechanisms
    Gunnar Kleinau
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    Endocr Rev 30:133-51. 2009
    ..Finally, we address the issue of structural implications and suggest a refined scenario for the initial signaling process on GPHRs...
  30. ncbi Pharmacochaperones post-translationally enhance cell surface expression by increasing conformational stability of wild-type and mutant vasopressin V2 receptors
    Stefan Wüller
    Forschungsinstitut fur Molekulare Pharmakologie, Campus Berlin Buch, Robert Roessle Str 10, 13125 Berlin, Germany
    J Biol Chem 279:47254-63. 2004
    ..The mechanisms involved in successful rescue of cell surface delivery are explained in a three-dimensional homology model of the antagonist-bound hV2R...
  31. doi Determinants contributing to claudin ion channel formation
    Anna Veshnyakova
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    Ann N Y Acad Sci 1257:45-53. 2012
    ....
  32. pmc The Pseudo signal peptide of the corticotropin-releasing factor receptor type 2A prevents receptor oligomerization
    Anke Teichmann
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
    J Biol Chem 287:27265-74. 2012
    ..Thus, we have identified a novel functional domain within the GPCR protein family, which plays a role in receptor oligomerization and which may be useful to study the functional significance of this process in general...
  33. doi Research resource: Update and extension of a glycoprotein hormone receptors web application
    Annika Kreuchwig
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
    Mol Endocrinol 25:707-12. 2011
    ..The web application "Sequence-Structure-Function-Analysis of GPHRs" is accessible on the internet at http://www.ssfa-gphr.de/...
  34. ncbi The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family
    Christian Kohler
    Department of NMR Supported Structural Biology, Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    J Struct Funct Genomics 7:131-8. 2006
    ..A structural comparison to entries of the PDB reveals a frequent domain with low sequence homology annotated as HMA and P-II domains in Pfam...
  35. ncbi The tight junction protein occludin and the adherens junction protein alpha-catenin share a common interaction mechanism with ZO-1
    Sebastian L Müller
    Forschungsinstitut fur Molekulare Pharmakologie, 13125 Berlin, Charite Campus Mitte, 10117 Berlin, Germany, and Charité Campus Benjamin Franklin, 12203 Berlin, Germany
    J Biol Chem 280:3747-56. 2005
    ....
  36. pmc Extended and structurally supported insights into extracellular hormone binding, signal transduction and organization of the thyrotropin receptor
    Gerd Krause
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    PLoS ONE 7:e52920. 2012
    ..This event triggers conformational changes at a convergent center of the LRRD and the hinge region, activating an "intramolecular agonistic unit" close to the transmembrane domain...
  37. pmc On the interaction of Clostridium perfringens enterotoxin with claudins
    Anna Veshnyakova
    Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    Toxins (Basel) 2:1336-56. 2010
    ..The results promote the development of recombinant cCPE-proteins and CPE-based peptidomimetics to modulate tight junctions for improved drug delivery or to treat tumors overexpressing claudins...
  38. pmc GPCR-SSFE: a comprehensive database of G-protein-coupled receptor template predictions and homology models
    Catherine L Worth
    Leibniz Institut fur Molekulare Pharmakologie, 13125 Berlin, Germany
    BMC Bioinformatics 12:185. 2011
    ..Here, we present a comprehensive database called the GPCR-SSFE, which provides initial homology models of the transmembrane helices for a large variety of family A GPCRs...
  39. ncbi The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology
    Dietmar Leitner
    Forschungsinstitut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
    FEBS Lett 579:3534-8. 2005
    ..Residues which are important for the heterodimerization with BEM1p are structurally preserved...
  40. ncbi Variant amino acids in the extracellular loops of murine and human vasopressin V2 receptors account for differences in cell surface expression and ligand affinity
    Alexander Oksche
    Forschungsinstitut fur Molekulare Pharmakologie, D 13125 Berlin, Germany
    Mol Endocrinol 16:799-813. 2002
    ..Thus, a single amino acid difference in the first extracellular loop between mV(2)R and hV(2)R determines the efficiency of cell surface expression...
  41. doi Functional significance of cleavable signal peptides of G protein-coupled receptors
    Ralf Schulein
    Leibniz Institut fur Molekulare Pharmakologie FMP, Robert Rossle Str 10, 13125 Berlin, Germany
    Eur J Cell Biol 91:294-9. 2012
    ..In this review, we summarize the current knowledge about cleavable signal peptides of GPCRs and address the question whether these sequences may be future drug targets in pharmacology...
  42. pmc Chemogenomic analysis of G-protein coupled receptors and their ligands deciphers locks and keys governing diverse aspects of signalling
    Jörg D Wichard
    Leibniz Institut fur Molekulare Pharmakologie, Berlin, Germany
    PLoS ONE 6:e16811. 2011
    ..Above all, the MI analysis provides detailed indications about amino acids located in the transmembrane region of these receptors that determine G-protein signalling pathway preferences...
  43. doi Histidines in potential substrate recognition sites affect thyroid hormone transport by monocarboxylate transporter 8 (MCT8)
    Doreen Braun
    Institut für Experimentelle Endokrinologie, Charite Universitatsmedizin Berlin, D 13353, Berlin, Germany
    Endocrinology 154:2553-61. 2013
    ..Molecular modeling demonstrates a perfect fit of T3 poised into the substrate channel between His415 and Arg301 and observing the same geometry as in the T3 receptor. ..
  44. ncbi The signal peptide of the G protein-coupled human endothelin B receptor is necessary for translocation of the N-terminal tail across the endoplasmic reticulum membrane
    Robert Köchl
    Forschungsinstitut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, USA
    J Biol Chem 277:16131-8. 2002
    ..We postulate that signal peptides are necessary for those G protein-coupled receptors for which post-translational translocation of the N terminus is impaired or blocked by the presence of stably folded domains...