3vrp: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 3vrp is ON HOLD
+==Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with phospho-EGFR peptide==
+<StructureSection load='3vrp' size='340' side='right'caption='[[3vrp]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3vrp]] 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=3VRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VRP FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=3vrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrp OCA], [https://pdbe.org/3vrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vrp RCSB], [https://www.ebi.ac.uk/pdbsum/3vrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vrp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CBLC_HUMAN CBLC_HUMAN] Regulator of EGFR mediated signal transduction.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Through their ubiquitin ligase activity, Cbl-family proteins suppress signalling mediated by protein-tyrosine kinases (PTKs), but can also function as adaptor proteins to positively regulate signalling. The tyrosine kinase binding (TKB) domain of this family is critical for binding with tyrosine-phosphorylated target proteins. Here, we analysed the crystal structure of the TKB domain of Cbl-c/Cbl-3 (Cbl-c TKB), which is a distinct member of the mammalian Cbl-family. In comparison with Cbl TKB, Cbl-c TKB showed restricted structural flexibility upon phosphopeptide binding. A mutation in Cbl-c TKB augmenting this flexibility enhanced its binding to target phosphoproteins. These results suggest that proteins, post-translational modifications or mutations that alter structural flexibility of the TKB domain of Cbl-family proteins could regulate their binding to target phosphoproteins and thereby, affect PTK-mediated signalling.
-Authors: Takeshita, K., Tezuka, T., Isozaki, Y., Yamashita, E., Suzuki, M., Yamanashi, Y., Yamamoto, T., Nakagawa, A.
+Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.,Takeshita K, Tezuka T, Isozaki Y, Yamashita E, Suzuki M, Kim M, Yamanashi Y, Yamamoto T, Nakagawa A J Biochem. 2012 Nov;152(5):487-95. doi: 10.1093/jb/mvs085. Epub 2012 Aug 9. PMID:22888118<ref>PMID:22888118</ref>
-Description: Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with phospho-EGFR peptide
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3vrp" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Isozaki Y]]
+[[Category: Nakagawa A]]
+[[Category: Suzuki M]]
+[[Category: Takeshita K]]
+[[Category: Tezuka T]]
+[[Category: Yamamoto T]]
+[[Category: Yamanashi Y]]
+[[Category: Yamashita E]]