1fmk

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(New page: 200px<br /> <applet load="1fmk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmk, resolution 1.5&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC'''<br />
'''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1FMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FMK OCA].
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1FMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMK OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Transferase]]
[[Category: Transferase]]
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[[Category: Eck, M.J.]]
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[[Category: Eck, M J.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
[[Category: Xu, W.]]
[[Category: Xu, W.]]
[[Category: phosphorylation]]
[[Category: phosphorylation]]
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[[Category: tyrosine kinase]]
[[Category: tyrosine kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:55:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:13 2008''

Revision as of 10:40, 21 February 2008


1fmk, resolution 1.5Å

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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. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 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

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