|
|
| (2 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| | |
| ==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 [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VRQ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3vrq]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39Å</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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=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> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vrq RCSB], [http://www.ebi.ac.uk/pdbsum/3vrq PDBsum]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CBLC_HUMAN CBLC_HUMAN]] Regulator of EGFR mediated signal transduction. | | [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.
| |
| | |
| 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>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Isozaki, Y]] | | [[Category: Large Structures]] |
| [[Category: Nakagawa, A]] | | [[Category: Isozaki Y]] |
| [[Category: Suzuki, M]] | | [[Category: Nakagawa A]] |
| [[Category: Takeshita, K]] | | [[Category: Suzuki M]] |
| [[Category: Tezuka, T]] | | [[Category: Takeshita K]] |
| [[Category: Yamamoto, T]] | | [[Category: Tezuka T]] |
| [[Category: Yamanashi, Y]] | | [[Category: Yamamoto T]] |
| [[Category: Yamashita, E]] | | [[Category: Yamanashi Y]] |
| [[Category: Calcium-binding ef hand]]
| | [[Category: Yamashita E]] |
| [[Category: Divergent sh2 domain]]
| |
| [[Category: Protein binding]]
| |
| [[Category: Ptb domain]]
| |
| [[Category: Regulator of egfr mediated signal transduction]]
| |
| [[Category: Ubiquitously expressed]]
| |