1ri9
From Proteopedia
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- | [[Image:1ri9.png|left|200px]] | ||
- | + | ==Structure of a helically extended SH3 domain of the T cell adapter protein ADAP== | |
+ | <StructureSection load='1ri9' size='340' side='right'caption='[[1ri9]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1ri9]] is a 1 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=1RI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RI9 FirstGlance]. <br> | ||
+ | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ri9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri9 OCA], [https://pdbe.org/1ri9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ri9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ri9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ri9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/FYB1_HUMAN FYB1_HUMAN] Congenital autosomal recessive small-platelet thrombocytopenia. The disease is caused by variants affecting the gene represented in this entry. | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/FYB1_HUMAN FYB1_HUMAN] Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).[UniProtKB:D3ZIE4][UniProtKB:O35601]<ref>PMID:10747096</ref> <ref>PMID:15849195</ref> <ref>PMID:16980616</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1ri9_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ri9 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The adapter protein ADAP (FYB/SLAP-130) provides a critical link between T cell receptor (TCR) signaling and cell adhesion via the activation of integrins. The C-terminal 70 residues of ADAP show homology to SH3 domains; however, conserved residues of the fold are absent. An alignment and annotation of this domain has therefore been elusive. We have solved the three-dimensional structure of the ADAP C-terminal domain by NMR spectroscopy and show that it represents an altered SH3 domain fold. An N-terminal, amphipathic helix makes extensive contacts to residues of the regular SH3 domain fold, and thereby a composite surface with unusual surface properties is created. 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. | ||
- | + | Structure of a helically extended SH3 domain of the T cell adapter protein ADAP.,Heuer K, Kofler M, Langdon G, Thiemke K, Freund C Structure. 2004 Apr;12(4):603-10. PMID:15062083<ref>PMID:15062083</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1ri9" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Freund | + | [[Category: Large Structures]] |
- | [[Category: Heuer | + | [[Category: Freund C]] |
- | [[Category: Kofler | + | [[Category: Heuer K]] |
- | [[Category: Langdon | + | [[Category: Kofler M]] |
- | [[Category: Thiemke | + | [[Category: Langdon G]] |
- | + | [[Category: Thiemke K]] | |
- | + | ||
- | + |
Current revision
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
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Categories: Homo sapiens | Large Structures | Freund C | Heuer K | Kofler M | Langdon G | Thiemke K