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1wyx

From Proteopedia

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(New page: 200px<br /> <applet load="1wyx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wyx, resolution 1.14&Aring;" /> '''The Crystal Structu...)
Current revision (13:35, 13 March 2024) (edit) (undo)
 
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[[Image:1wyx.gif|left|200px]]<br />
 
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<applet load="1wyx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wyx, resolution 1.14&Aring;" />
 
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'''The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution'''<br />
 
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==Overview==
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==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==
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The Crk-associated tyrosine kinase substrate p130cas (CAS) is a docking, protein containing an SH3 domain near its N terminus, followed by a short, proline-rich segment, a large central substrate domain composed of 15, repeats of the four amino acid sequence YxxP, a serine-rich region and a, carboxy-terminal domain, which possesses consensus binding sites for the, SH2 and SH3 domains of Src (YDYV and RPLPSPP, respectively). The SH3, domain of CAS mediates its interaction with several proteins involved in, signaling pathways such as focal adhesion kinase (FAK), tyrosine, phosphatases PTP1B and PTP-PEST, and the guanine nucleotide exchange, factor C3G. As a homolog of the corresponding Src docking domain, the CAS, SH3 domain binds to proline-rich sequences (PxxP) of its interacting, partners that can adopt a polyproline type II helix. We have determined a, high-resolution X-ray structure of the recombinant human CAS SH3 domain., The domain, residues 1-69, crystallized in two related space groups, P2(1), and C222(1), that provided diffraction data to 1.1 A and 2.1 A, respectively. The crystal structure shows, in addition to the conserved, SH3 domain architecture, the way in which the CAS characteristic amino, acids form an atypically charged ligand-binding surface. This arrangement, provides a rationale for the unusual ligand recognition motif exhibited by, the CAS SH3 domain. The structure enables modelling of the docking, interactions to its ligands, for example from focal adhesion kinase, and, supports structure-based drug design of inhibitors of the CAS-FAK, interaction.
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<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1wyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
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Known diseases associated with this structure: Albinism, brown OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=115501 115501]], Albinism, rufous OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=115501 115501]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==About this Structure==
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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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [https://pdbe.org/1wyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [https://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx ProSAT]</span></td></tr>
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1WYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WYX OCA].
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</table>
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== Function ==
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==Reference==
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[https://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>
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The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity., Wisniewska M, Bossenmaier B, Georges G, Hesse F, Dangl M, Kunkele KP, Ioannidis I, Huber R, Engh RA, J Mol Biol. 2005 Apr 15;347(5):1005-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15784259 15784259]
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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/wy/1wyx_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=1wyx ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Bossenmaier, B.]]
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[[Category: Bossenmaier B]]
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[[Category: Dangl, M.]]
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[[Category: Dangl M]]
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[[Category: Engh, R.A.]]
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[[Category: Engh RA]]
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[[Category: Georges, G.]]
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[[Category: Georges G]]
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[[Category: Hesse, F.]]
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[[Category: Hesse F]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Ioannidis, I.]]
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[[Category: Ioannidis I]]
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[[Category: Kuenkele, K.P.]]
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[[Category: Kuenkele KP]]
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[[Category: Wisniewska, M.]]
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[[Category: Wisniewska M]]
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[[Category: EDO]]
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[[Category: MG]]
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[[Category: beta sheets]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:56:51 2007''
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Current revision

The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution

PDB ID 1wyx

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