1fmk: Difference between revisions
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'''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC''' | '''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC''' | ||
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[[Category: Harrison, S C.]] | [[Category: Harrison, S C.]] | ||
[[Category: Xu, W.]] | [[Category: Xu, W.]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
[[Category: | [[Category: Phosphotransferase]] | ||
[[Category: | [[Category: Phosphotyrosine]] | ||
[[Category: | [[Category: Proto-oncogene]] | ||
[[Category: | [[Category: Sh2]] | ||
[[Category: | [[Category: Sh3]] | ||
[[Category: | [[Category: Src]] | ||
[[Category: | [[Category: Tyrosine kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:30:20 2008'' | |||
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Revision as of 16:30, 2 May 2008
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
OverviewOverview
The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase.
About this StructureAbout this Structure
1FMK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the tyrosine kinase c-Src., Xu W, Harrison SC, Eck MJ, Nature. 1997 Feb 13;385(6617):595-602. PMID:9024657 Page seeded by OCA on Fri May 2 16:30:20 2008