1b07

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[[Image:1b07.png|left|200px]]
 
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{{STRUCTURE_1b07| PDB=1b07 | SCENE= }}
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==CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR==
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<StructureSection load='1b07' size='340' side='right'caption='[[1b07]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B07 FirstGlance]. <br>
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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]] 2.5&#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=PYJ:PHENYLETHANE'>PYJ</scene></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=1b07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b07 OCA], [https://pdbe.org/1b07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b07 RCSB], [https://www.ebi.ac.uk/pdbsum/1b07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b07 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRK_MOUSE CRK_MOUSE] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.
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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/b0/1b07_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1b07 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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Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity.
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===CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR===
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Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors.,Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931<ref>PMID:9851931</ref>
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{{ABSTRACT_PUBMED_9851931}}
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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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==About this Structure==
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<div class="pdbe-citations 1b07" style="background-color:#fffaf0;"></div>
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[[1b07]] is a 2 chain structure of [[Non-Standard Residue]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B07 OCA].
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==See Also==
==See Also==
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*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
*[[Non-Standard Residue|Non-Standard Residue]]
*[[Non-Standard Residue|Non-Standard Residue]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:009851931</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Cohen, F E.]]
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[[Category: Cohen FE]]
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[[Category: Lim, W A.]]
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[[Category: Lim WA]]
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[[Category: Nguyen, J T.]]
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[[Category: Nguyen JT]]
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[[Category: Turck, C W.]]
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[[Category: Turck CW]]
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[[Category: Zuckermann, R N.]]
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[[Category: Zuckermann RN]]
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[[Category: Inhibitor]]
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[[Category: Peptoid]]
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[[Category: Proline-rich motif]]
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[[Category: Protein-protein recognition]]
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[[Category: Sh3 domain]]
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[[Category: Signal transduction]]
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Current revision

CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

PDB ID 1b07

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