2eyw: Difference between revisions
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'''N-terminal SH3 domain of CT10-Regulated Kinase'''<br /> | '''N-terminal SH3 domain of CT10-Regulated Kinase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2EYW is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: sh3]] | [[Category: sh3]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:57:37 2008'' | ||
Revision as of 15:57, 23 January 2008
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N-terminal SH3 domain of CT10-Regulated Kinase
OverviewOverview
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 StructureAbout this Structure
2EYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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