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| | ==CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide== | | ==CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide== |
| - | <StructureSection load='1l2z' size='340' side='right' caption='[[1l2z]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1l2z' size='340' side='right'caption='[[1l2z]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l2z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1l2z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2Z FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gyf|1gyf]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD2BP2 (amino acids 280-341) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2z OCA], [https://pdbe.org/1l2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2z RCSB], [https://www.ebi.ac.uk/pdbsum/1l2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2z ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2z OCA], [http://pdbe.org/1l2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l2z RCSB], [http://www.ebi.ac.uk/pdbsum/1l2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CD2_HUMAN CD2_HUMAN]] CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. | + | [https://www.uniprot.org/uniprot/CD2B2_HUMAN CD2B2_HUMAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Freund, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Kuhne, R]] | + | [[Category: Freund C]] |
| - | [[Category: Park, S]] | + | [[Category: Kuhne R]] |
| - | [[Category: Reinherz, E L]] | + | [[Category: Park S]] |
| - | [[Category: Wagner, G]] | + | [[Category: Reinherz EL]] |
| - | [[Category: Yang, H]] | + | [[Category: Wagner G]] |
| - | [[Category: Cd2]]
| + | [[Category: Yang H]] |
| - | [[Category: Cd2bp2]]
| + | |
| - | [[Category: Gyf domain]]
| + | |
| - | [[Category: Peptide binding-signaling protein complex]]
| + | |
| - | [[Category: Proline-rich peptide]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| Structural highlights
Function
CD2B2_HUMAN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Intracellular protein interaction domains are essential for eukaryotic signaling. In T cells, the CD2BP2 adaptor binds two membrane-proximal proline-rich motifs in the CD2 cytoplasmic tail via its GYF domain, thereby regulating interleukin-2 production. Here we present the structure of the GYF domain in complex with a CD2 tail peptide. Unlike SH3 domains, which use two surface pockets to accommodate proline residues of ligands, the GYF domain employs phylogenetically conserved hydrophobic residues to create a single interaction surface. NMR analysis shows that the Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. This unveils the mechanism of a switch of CD2 function due to an extracellular mitogenic signal.
Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules.,Freund C, Kuhne R, Yang H, Park S, Reinherz EL, Wagner G EMBO J. 2002 Nov 15;21(22):5985-95. PMID:12426371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Freund C, Kuhne R, Yang H, Park S, Reinherz EL, Wagner G. Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules. EMBO J. 2002 Nov 15;21(22):5985-95. PMID:12426371
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