Research Topics
Genomes and Genes | Christian FreundSummaryCountry: Germany Publications
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Publications
Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector moleculesChristian Freund
Protein Engineering Group and Molecular Modeling Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Strasse 10, D 13125 Berlin, Germany
EMBO J 21:5985-95. 2002..This unveils the mechanism of a switch of CD2 function due to an extracellular mitogenic signal...
Structural investigations of a GYF domain covalently linked to a proline-rich peptideChristian Freund
Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Biomol NMR 27:143-9. 2003..In conjunction with general recognition rules for proline-rich sequence recognition these NOEs allowed the accurate modeling of the protein-peptide complex...- GYF domain proteomics reveals interaction sites in known and novel target proteinsMichael Kofler
Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Str 10, 13125 Berlin, Germany
Mol Cell Proteomics 4:1797-811. 2005..The binding epitope of the GYF domain from the yeast SMY2 protein was mapped by NMR spectroscopy and led to a structural model that accounts for the different binding properties of SMY2-type GYF domains and the CD2BP2-GYF domain... - Novel interaction partners of the CD2BP2-GYF domainMichael Kofler
Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Biol Chem 280:33397-402. 2005..A direct interaction of the CD2BP2-GYF domain with the novel protein interaction partners PI31 and NPWBP was verified by yeast two-hybrid analysis... - Proline-rich sequence recognition: II. Proteomics analysis of Tsg101 ubiquitin-E2-like variant (UEV) interactionsAndreas Schlundt
Protein Engineering Group, Leibniz Institute for Molecular Pharmacology and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
Mol Cell Proteomics 8:2474-86. 2009..Mol. Cell. Proteomics 8, 2461-2473) on GYF and WW domain pathways our work defines major proline-rich sequence-mediated interaction networks that contribute to the modular assembly of physiologically relevant protein complexes... 
Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexesMiriam Rose Ash
Protein Engineering, Leibniz Institut fuer Molekulare Pharmakologie, 13125 Berlin, Germany
Structure 18:944-54. 2010..The current study highlights the structural basis for PRS recognition by Smy2-type GYF domains, and implicates Smy2 and GIGYF2 in both mRNA processing and the secretory pathway...- Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2Michael Kofler
Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie und Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Biol Chem 279:28292-7. 2004..The colocalization of CD2BP2 and SmB proteins in the nucleus of Jurkat T cells and HeLa cells suggests a function of the GYF domain of CD2BP2 in mediating protein-protein interactions within the spliceosome... - Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cellsMarc Sylvester
Protein Engineering Group, Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
PLoS ONE 5:e11708. 2010.... - Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexesMichael Kofler
Protein Engineering Group, Leibniz Institute for Molecular Pharmacology and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
Mol Cell Proteomics 8:2461-73. 2009..Saturating the PRS sites by an isolated GYF domain inhibited splicing at the level of A complex formation. The interactions mediated by PRS are therefore important to the early phases of spliceosomal assembly... - Redox-regulated conformational changes in an SH3 domainJurgen Zimmermann
Protein Engineering Group, Leibniz Institut für Molekulare Pharmakologie und Freie Universität Berlin, 13125 Berlin, Germany
Biochemistry 46:6971-7. 2007..The redox potential for this structural transition is -228 mV at pH 7.4. This is compatible with a role of the cysteinylcysteine moiety in redox signaling during T cell activation... - Lipid-binding hSH3 domains in immune cell adapter proteinsKatja Heuer
Protein Engineering Group, Leibniz Institute of Molecular Pharmacology and Freie Universität Berlin, Germany
J Mol Biol 361:94-104. 2006..Functional investigations indicate that deletion of both amphipathic helices of the hSH3 domains reduces the ability of ADAP to enhance adhesion and migration in stimulated T cells... - Multivalent binding of formin-binding protein 21 (FBP21)-tandem-WW domains fosters protein recognition in the pre-spliceosomeStefan Klippel
Protein Engineering Group, Leibniz Institut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Biol Chem 286:38478-87. 2011..This suggests that distinct orientations of the ligand contribute to a delocalized and semispecific binding mode that should facilitate search processes within the spliceosome... - Improved two-dimensional reversed phase-reversed phase LC-MS/MS approach for identification of peptide-protein interactionsHeike Stephanowitz
Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Str 10, 13125 Berlin, Germany
J Proteome Res 11:1175-83. 2012..From a technical point of view we provide a detailed protocol for an offline 2-D RP-RP LC-MS/MS method that offers a robust and time-saving alternative for quantitative interactome analysis... - Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopyKirill Piotukh
Leibniz Institute for Molecular Pharmacology and Freie Universität Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
Free Radic Biol Med 43:1263-70. 2007..Redox potentials can be measured accurately in homogeneous solutions and define the conditions under which regulatory oxidation of the respective protein may occur in the living cell... - Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteinsKirill Piotukh
Protein Engineering Group, Freie Universität Berlin and Forschungsinstitut für Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Biol Chem 280:23668-74. 2005..These sequences represent putative target sites for binding of CypA to intracellular proteins... - The GYF domainMichael M Kofler
Protein Engineering Group, Free University and FMP Berlin, Germany
FEBS J 273:245-56. 2006..Thereby proteomics has contributed to a functional understanding of GYF domain-containing proteins and sets the stage for a more systematic investigation of their functions in vivo... - Investigating the functional role of CD2BP2 in T cellsMatthias Heinze
Protein Engineering Group, Leibniz Institute of Molecular Pharmacology and Free University Berlin, Robert Rossle Strasse 10, 13125 Berlin, Germany
Int Immunol 19:1313-8. 2007..No major difference in cytokine expression can be observed for primary cells transfected with CD2BP2-specific small interfering RNA. We conclude that CD2 signaling is at least partially independent of its in vitro binding partner CD2BP2... - Bidirectional binding of invariant chain peptides to an MHC class II moleculeSebastian Günther
Leibniz Institute for Molecular Pharmacology and Freie Universität Berlin, 13125 Berlin, Germany
Proc Natl Acad Sci U S A 107:22219-24. 2010..Thus, noncanonical MHC-CLIP displays the hallmarks of a structurally and functionally intact antigen-presenting complex... - The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domainKatja Heuer
Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Str 10, 13125 Berlin, Germany
J Mol Biol 348:1025-35. 2005..Furthermore, the ADAP lipid interaction defines the helically extended SH3 scaffold as a novel member of membrane interaction domains... - A novel hSH3 domain scaffold engineered to bind folded domains in CD2BP2 and HIV capsid proteinKirill Piotukh
Leibniz Institute for Molecular Pharmacology Robert Rössle Str 10, 13125 Berlin, Germany
Protein Eng Des Sel 25:649-56. 2012..The soluble scaffolds bind with 340 and 600 nM affinity to CA and CD2BP2, respectively, and employ large molecular surfaces to pull out these targets from complex mixtures... 
Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequenceDoreen Pahlke
Forschungsinstitut für Molekulare Pharmakologie Robert Rössle Str 10, D 13125 Berlin, Germany
BMC Struct Biol 5:8. 2005..Furthermore we analyzed the relationship between the relative solvent accessibility and the relative occurrence of prolines in the cis and in the trans conformation...- Structure of a helically extended SH3 domain of the T cell adapter protein ADAPKatja Heuer
Protein Engineering Group, , , 13125 Berlin, Germany
Structure 12:603-10. 2004..We propose this SH3 domain variant to be classified as a helically extended SH3 domain (hSH3 domain) and show that the ADAP-hSH3 domain can no longer bind conventional proline-rich peptides... - Directed evolution of sortase A mutants with altered substrate selectivity profilesKirill Piotukh
Department of Protein Engineering, Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
J Am Chem Soc 133:17536-9. 2011..Our report is a decisive step toward a platform of engineered sortases with distinct ligation properties that will conceivably allow for more versatile assemblies of modified proteins in biotechnological approaches... - A xenon-129 biosensor for monitoring MHC-peptide interactionsAndreas Schlundt
Protein Engineering Group, Leibniz Institut für Molekulare Pharmakologie und FU Berlin, Robert Roessle Strasse 10, 13125 Berlin, Germany
Angew Chem Int Ed Engl 48:4142-5. 2009..Cryptophane molecules that trap Xe atoms are modified with a hemagglutinin (HA) peptide, which binds to the MHC protein. The interaction can be monitored by an NMR chemical shift change of cage-HA bound (129)Xe... - Alternative binding modes of proline-rich peptides binding to the GYF domainWei Gu
Zentrum fur Bioinformatik, Universitat des Saarlandes, D 66041 Saarbrucken, Germany
Biochemistry 44:6404-15. 2005..Possible functional implications of this altered conformation of the bound ligand are discussed in the light of our experimental and theoretical results... - The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1Stefanie Kliche
Institute of Immunology, Otto von Guericke University, 39120 Magdeburg, Germany
Mol Cell Biol 26:7130-44. 2006..However, it appears as if the ADAP/SKAP55 module can exert its signaling function outside of the classical raft fraction of the cell membrane... - NMR assignment of the reduced and oxidized forms of the human ADAP hSH3-1 domainJurgen Zimmermann
J Biomol NMR 32:94. 2005 - Analysis of the substrate specificity of the Dim-5 histone lysine methyltransferase using peptide arraysPhilipp Rathert
Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany
Chem Biol 15:5-11. 2008..Comparative analyses of peptide arrays with wild-type and mutant enzymes, therefore, are well suited to investigate the target specificity of protein methyltransferases and study epigenetic crosstalk...