3vrq: Difference between revisions
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==Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)== | ==Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)== | ||
<StructureSection load='3vrq' size='340' side='right' caption='[[3vrq]], [[Resolution|resolution]] 2.39Å' scene=''> | <StructureSection load='3vrq' size='340' side='right'caption='[[3vrq]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vrq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vrq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VRQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vrn|3vrn]], [[3vro|3vro]], [[3vrp|3vrp]], [[3vrr|3vrr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vrn|3vrn]], [[3vro|3vro]], [[3vrp|3vrp]], [[3vrr|3vrr]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBLC ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBLC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrq OCA], [https://pdbe.org/3vrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vrq RCSB], [https://www.ebi.ac.uk/pdbsum/3vrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vrq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CBLC_HUMAN CBLC_HUMAN]] Regulator of EGFR mediated signal transduction. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Isozaki, Y]] | [[Category: Isozaki, Y]] | ||
[[Category: Nakagawa, A]] | [[Category: Nakagawa, A]] | ||
Revision as of 22:00, 27 July 2022
Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)
Structural highlights
Function[CBLC_HUMAN] Regulator of EGFR mediated signal transduction. Publication Abstract from PubMedThrough 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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