1m30: Difference between revisions
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==Solution structure of N-terminal SH3 domain from oncogene protein c-Crk== | ==Solution structure of N-terminal SH3 domain from oncogene protein c-Crk== | ||
<StructureSection load='1m30' size='340' side='right'caption='[[1m30 | <StructureSection load='1m30' size='340' side='right'caption='[[1m30]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m30]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1m30]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M30 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1m30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m30 OCA], [https://pdbe.org/1m30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m30 RCSB], [https://www.ebi.ac.uk/pdbsum/1m30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m30 ProSAT]</span></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=1m30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m30 OCA], [https://pdbe.org/1m30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m30 RCSB], [https://www.ebi.ac.uk/pdbsum/1m30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m30 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Camarero | [[Category: Camarero JA]] | ||
[[Category: Fushman | [[Category: Fushman D]] | ||
[[Category: Hall | [[Category: Hall JB]] | ||
[[Category: Schumann | [[Category: Schumann FH]] | ||
[[Category: Tayakuniyil | [[Category: Tayakuniyil PP]] | ||
[[Category: Varadan | [[Category: Varadan R]] | ||
Latest revision as of 11:30, 10 April 2024
Solution structure of N-terminal SH3 domain from oncogene protein c-CrkSolution structure of N-terminal SH3 domain from oncogene protein c-Crk
Structural highlights
FunctionCRK_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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