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1ri9

From Proteopedia

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{{Seed}}
 
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[[Image:1ri9.png|left|200px]]
 
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==Structure of a helically extended SH3 domain of the T cell adapter protein ADAP==
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The line below this paragraph, containing "STRUCTURE_1ri9", creates the "Structure Box" on the page.
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<StructureSection load='1ri9' size='340' side='right'caption='[[1ri9]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_1ri9| PDB=1ri9 | SCENE= }}
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1ri9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structure of a helically extended SH3 domain of the T cell adapter protein ADAP===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1ri9" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15062083 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15062083}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1RI9 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15062083 15062083]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Freund, C.]]
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[[Category: Freund C]]
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[[Category: Heuer, K.]]
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[[Category: Heuer K]]
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[[Category: Kofler, M.]]
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[[Category: Kofler M]]
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[[Category: Langdon, G.]]
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[[Category: Langdon G]]
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[[Category: Thiemke, K.]]
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[[Category: Thiemke K]]
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[[Category: Helically extended]]
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[[Category: Sh3-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:14:57 2008''
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Current revision

Structure of a helically extended SH3 domain of the T cell adapter protein ADAP

PDB ID 1ri9

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