Christian Freund

Summary

Country: Germany

Publications

  1. pmc Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules
    Christian 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
  2. ncbi request reprint Structural investigations of a GYF domain covalently linked to a proline-rich peptide
    Christian 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
  3. ncbi request reprint GYF domain proteomics reveals interaction sites in known and novel target proteins
    Michael 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
  4. ncbi request reprint Novel interaction partners of the CD2BP2-GYF domain
    Michael 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
  5. pmc Proline-rich sequence recognition: II. Proteomics analysis of Tsg101 ubiquitin-E2-like variant (UEV) interactions
    Andreas 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
  6. doi request reprint Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes
    Miriam Rose Ash
    Protein Engineering, Leibniz Institut fuer Molekulare Pharmakologie, 13125 Berlin, Germany
    Structure 18:944-54. 2010
  7. ncbi request reprint Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2
    Michael 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
  8. pmc Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells
    Marc Sylvester
    Protein Engineering Group, Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
    PLoS ONE 5:e11708. 2010
  9. pmc Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes
    Michael 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
  10. ncbi request reprint Redox-regulated conformational changes in an SH3 domain
    Jurgen Zimmermann
    Protein Engineering Group, Leibniz Institut für Molekulare Pharmakologie und Freie Universität Berlin, 13125 Berlin, Germany
    Biochemistry 46:6971-7. 2007

Collaborators

Detail Information

Publications29

  1. pmc Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules
    Christian 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...
  2. ncbi request reprint Structural investigations of a GYF domain covalently linked to a proline-rich peptide
    Christian 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...
  3. ncbi request reprint GYF domain proteomics reveals interaction sites in known and novel target proteins
    Michael 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...
  4. ncbi request reprint Novel interaction partners of the CD2BP2-GYF domain
    Michael 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...
  5. pmc Proline-rich sequence recognition: II. Proteomics analysis of Tsg101 ubiquitin-E2-like variant (UEV) interactions
    Andreas 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...
  6. doi request reprint Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes
    Miriam 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...
  7. ncbi request reprint Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2
    Michael 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...
  8. pmc Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells
    Marc Sylvester
    Protein Engineering Group, Leibniz Institut fur Molekulare Pharmakologie FMP, Berlin, Germany
    PLoS ONE 5:e11708. 2010
    ....
  9. pmc Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes
    Michael 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...
  10. ncbi request reprint Redox-regulated conformational changes in an SH3 domain
    Jurgen 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...
  11. ncbi request reprint Lipid-binding hSH3 domains in immune cell adapter proteins
    Katja 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...
  12. pmc Multivalent binding of formin-binding protein 21 (FBP21)-tandem-WW domains fosters protein recognition in the pre-spliceosome
    Stefan 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...
  13. doi request reprint Improved two-dimensional reversed phase-reversed phase LC-MS/MS approach for identification of peptide-protein interactions
    Heike 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...
  14. ncbi request reprint Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy
    Kirill 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...
  15. ncbi request reprint Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins
    Kirill 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...
  16. ncbi request reprint The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain
    Katja 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...
  17. pmc Bidirectional binding of invariant chain peptides to an MHC class II molecule
    Sebastian 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...
  18. ncbi request reprint Investigating the functional role of CD2BP2 in T cells
    Matthias 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...
  19. ncbi request reprint The GYF domain
    Michael 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...
  20. ncbi request reprint A novel hSH3 domain scaffold engineered to bind folded domains in CD2BP2 and HIV capsid protein
    Kirill 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...
  21. pmc Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence
    Doreen 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...
  22. ncbi request reprint Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
    Katja Heuer
    Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert Rossle Strasse 10, 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...
  23. doi request reprint Directed evolution of sortase A mutants with altered substrate selectivity profiles
    Kirill 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...
  24. doi request reprint A xenon-129 biosensor for monitoring MHC-peptide interactions
    Andreas 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...
  25. doi request reprint Probing the recognition of post-translational modifications by combining sortase-mediated ligation and phage-assisted selection
    Till Teschke
    Departments of Protein Chemistry and Protein Engineering, Leibniz Institut fur Molekulare Pharmakologie, Robert Rossle Strasse 10, 13125 Berlin, Germany
    ACS Chem Biol 8:1692-7. 2013
    ..We have demonstrated the applicability of this method by probing the interaction of phosphorylated tyrosine and serine residues with their respective binding domains. ..
  26. ncbi request reprint Alternative binding modes of proline-rich peptides binding to the GYF domain
    Wei 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...
  27. pmc The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1
    Stefanie 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...
  28. ncbi request reprint NMR assignment of the reduced and oxidized forms of the human ADAP hSH3-1 domain
    Jurgen Zimmermann
    J Biomol NMR 32:94. 2005
  29. pmc Analysis of the substrate specificity of the Dim-5 histone lysine methyltransferase using peptide arrays
    Philipp 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...