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2fei

From Proteopedia

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[[Image:2fei.jpg|left|200px]]
 
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{{Structure
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==Solution structure of the second SH3 domain of Human CMS protein==
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|PDB= 2fei |SIZE=350|CAPTION= <scene name='initialview01'>2fei</scene>
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<StructureSection load='2fei' size='340' side='right'caption='[[2fei]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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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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|GENE= CMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=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>
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}}
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</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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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/fe/2fei_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=2fei 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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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.
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'''Solution structure of the second SH3 domain of Human CMS protein'''
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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>
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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>
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<div class="pdbe-citations 2fei" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[CD2-associated protein 3D structures|CD2-associated protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2FEI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEI OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17188587 17188587]
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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: Dai, H.]]
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[[Category: Dai H]]
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[[Category: Jiao, Y.]]
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[[Category: Jiao Y]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Wu, J.]]
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[[Category: Wu J]]
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[[Category: Yao, B.]]
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[[Category: Yao B]]
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[[Category: cms sh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:51:27 2008''
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Current revision

Solution structure of the second SH3 domain of Human CMS protein

PDB ID 2fei

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