5l23
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5l23 is ON HOLD Authors: Bhatt, V.S., Krieger, I., Sacchettini, J., Cho, J.-H. Description: Crystal structure of the complex between the N-terminal...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the complex between the N-terminal SH3 domain of CrkII and a proline-rich ligand== | |
| + | <StructureSection load='5l23' size='340' side='right'caption='[[5l23]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5l23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L23 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]] 1.77Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5l23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l23 OCA], [https://pdbe.org/5l23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l23 RCSB], [https://www.ebi.ac.uk/pdbsum/5l23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l23 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Cho | + | [[Category: Bhatt VS]] |
| - | [[Category: Krieger | + | [[Category: Cho J-H]] |
| + | [[Category: Krieger I]] | ||
| + | [[Category: Sacchettini J]] | ||
Current revision
Crystal structure of the complex between the N-terminal SH3 domain of CrkII and a proline-rich ligand
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