2fei
From Proteopedia
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| - | {{STRUCTURE_2fei| PDB=2fei | SCENE= }} | ||
| - | ===Solution structure of the second SH3 domain of Human CMS protein=== | ||
| - | {{ABSTRACT_PUBMED_17188587}} | ||
| - | == | + | ==Solution structure of the second SH3 domain of Human CMS protein== |
| - | [[http://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN | + | <StructureSection load='2fei' size='340' side='right'caption='[[2fei]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2fei]] 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=2FEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEI 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=2fei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fei OCA], [https://pdbe.org/2fei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fei RCSB], [https://www.ebi.ac.uk/pdbsum/2fei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fei ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN] Defects in CD2AP are the cause of susceptibility to focal segmental glomerulosclerosis type 3 (FSGS3) [MIM:[https://omim.org/entry/607832 607832]. A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and edema. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.<ref>PMID:12764198</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN] Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis.<ref>PMID:15800069</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/fe/2fei_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=2fei ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CMS, cas ligand with multiple Src homology 3 (SH3) domains, belongs to a family of ubiquitously expressed adaptor proteins. Among the CMS binding proteins, c-Cbl has been mostly extensively studied. It was reported that the motif PKPFPR (residues 824-829) of c-Cbl can bind to the N-terminus SH3 domains of CMS. Here we report the solution structure of the second SH3 domain of CMS (CMS_SH3_B), furthermore, we have identified that a peptide from residues 701 to 714 of c-Cbl (Cbl-p), i.e. MTPSSRPLRPLDTS, can specially bind to CMS_SH3_B using NMR chemical shift perturbation, suggesting that the peptide is a new potential CMS binding site. Among the peptide, TPSSRPLR is the core binding motif and Arg709 plays a key role in the interaction. Cbl-p binding interface on CMS_SH3_B along a hydrophobic channel is composed of RT loop, n-Src loop and beta4 strand and divided into three pockets. This work indicates the solution structure of CMS_SH3_B bears the canonical beta-beta-beta-beta-alpha-beta fold and a new binding site in c-Cbl involved in its interaction with CMS, which probably contributes to the clustering of CMS. All the information provided here should be beneficial for the future functional study of CMS. | ||
| - | + | Solution structure of the second SH3 domain of human CMS and a newly identified binding site at the C-terminus of c-Cbl.,Yao B, Zhang J, Dai H, Sun J, Jiao Y, Tang Y, Wu J, Shi Y Biochim Biophys Acta. 2007 Jan;1774(1):35-43. Epub 2006 Oct 27. PMID:17188587<ref>PMID:17188587</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2fei" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[CD2-associated protein 3D structures|CD2-associated protein 3D structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Dai | + | [[Category: Large Structures]] |
| - | [[Category: Jiao | + | [[Category: Dai H]] |
| - | [[Category: Shi | + | [[Category: Jiao Y]] |
| - | [[Category: Wu | + | [[Category: Shi Y]] |
| - | [[Category: Yao | + | [[Category: Wu J]] |
| - | + | [[Category: Yao B]] | |
| - | + | ||
Current revision
Solution structure of the second SH3 domain of Human CMS protein
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Categories: Homo sapiens | Large Structures | Dai H | Jiao Y | Shi Y | Wu J | Yao B
