1fmk
From Proteopedia
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[[Image:1fmk.gif|left|200px]] | [[Image:1fmk.gif|left|200px]] | ||
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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'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:30, 2 May 2008
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Overview
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 Structure
1FMK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Categories: Homo sapiens | Single protein | Transferase | Eck, M J. | Harrison, S C. | Xu, W. | Phosphorylation | Phosphotransferase | Phosphotyrosine | Proto-oncogene | Sh2 | Sh3 | Src | Tyrosine kinase