1fmk
From Proteopedia
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- | [[Image:1fmk.gif|left|200px]] | + | [[Image:1fmk.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC''' | + | {{Structure |
+ | |PDB= 1fmk |SIZE=350|CAPTION= <scene name='initialview01'>1fmk</scene>, resolution 1.5Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1FMK is a [ | + | 1FMK 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=1FMK OCA]. |
==Reference== | ==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:[http:// | + | Three-dimensional structure of the tyrosine kinase c-Src., Xu W, Harrison SC, Eck MJ, Nature. 1997 Feb 13;385(6617):595-602. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9024657 9024657] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tyrosine kinase]] | [[Category: tyrosine kinase]] | ||
- | ''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 11:11:04 2008'' |
Revision as of 09:11, 20 March 2008
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, resolution 1.5Å | |||||||
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Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Contents |
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.
Disease
Known disease associated with this structure: Colon cancer, advanced OMIM:[190090]
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 Thu Mar 20 11:11:04 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