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1m3c
From Proteopedia
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==Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk== | ==Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk== | ||
| - | <StructureSection load='1m3c' size='340' side='right'caption='[[1m3c | + | <StructureSection load='1m3c' size='340' side='right'caption='[[1m3c]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1m3c]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1m3c]] 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=1M3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M3C 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=1m3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m3c OCA], [https://pdbe.org/1m3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m3c RCSB], [https://www.ebi.ac.uk/pdbsum/1m3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m3c ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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]] |
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Current revision
Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk
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