2eyw
From Proteopedia
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| - | [[Image:2eyw.jpg|left|200px]] | + | [[Image:2eyw.jpg|left|200px]] |
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| - | '''N-terminal SH3 domain of CT10-Regulated Kinase''' | + | {{Structure |
| + | |PDB= 2eyw |SIZE=350|CAPTION= <scene name='initialview01'>2eyw</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''N-terminal SH3 domain of CT10-Regulated Kinase''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EYW is a [ | + | 2EYW is a [[Single protein]] structure of 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=2EYW OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK., Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F, Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:[http:// | + | Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK., Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F, Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17515907 17515907] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh3]] | [[Category: sh3]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:01 2008'' |
Revision as of 14:46, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-terminal SH3 domain of CT10-Regulated Kinase
Overview
CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK that regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. CRKI shows substantial transforming activity, whereas the activity of CRKII is low, and phosphorylated CRKII has no biological activity whatsoever. The molecular mechanisms underlying the distinct biological activities of the CRK proteins remain elusive. We determined the solution structures of CRKI, CRKII and phosphorylated CRKII by NMR and identified the molecular mechanism that gives rise to their activities. Results from mutational analysis using rodent 3Y1 fibroblasts were consistent with those from the structural studies. Together, these data suggest that the linker region modulates the binding of CRKII to its targets, thus regulating cell growth and motility.
About this Structure
2EYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK., Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F, Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:17515907
Page seeded by OCA on Thu Mar 20 16:46:01 2008
