1far

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(New page: 200px<br /> <applet load="1far" size="450" color="white" frame="true" align="right" spinBox="true" caption="1far" /> '''RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED ...)
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==About this Structure==
==About this Structure==
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1FAR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAR OCA]].
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1FAR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: ZN1 and ZN2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAR OCA]].
==Reference==
==Reference==
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:44:00 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:02:37 2007''

Revision as of 09:57, 30 October 2007


1far

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RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Overview

The Raf-1 protein kinase is the best-characterized downstream effector of, activated Ras. Interaction with Ras leads to Raf-1 activation and results, in transduction of cell growth and differentiation signals. The details of, Raf-1 activation are unclear, but our characterization of a second, Ras-binding site in the cysteine-rich domain (CRD) and the involvement of, both Ras-binding sites in effective Raf-1-mediated transformation provides, insight into the molecular aspects and consequences of Ras-Raf, interactions. The Raf-1 CRD is a member of an emerging family of domains, many of which are found within signal transducing proteins. Several, contain binding sites for diacylglycerol (or phorbol esters) and, phosphatidylserine and are believed to play a role in membrane, translocation and ... [(full description)]

About this Structure

1FAR is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Structure known Active Sites: ZN1 and ZN2. Full crystallographic information is available from [OCA].

Reference

The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site., Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL, Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8312-7. PMID:8710867

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