1far: Difference between revisions

Revision as of 02:58, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1far.png

Template:STRUCTURE 1far

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

Template:ABSTRACT PUBMED 8710867

About this StructureAbout this Structure

1FAR is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1far|  PDB=1far  |  SCENE=  }}
-'''RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
+===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 enzyme activation. The CRD from Raf-1 does not bind diacylglycerol but interacts with Ras and phosphatidylserine. To investigate the ligand-binding specificities associated with CRDs, we have determined the solution structure of the Raf-1 CRD using heteronuclear multidimensional NMR. We show that there are differences between this structure and the structures of two related domains from protein kinase C (PKC). The differences are confined to regions of the CRDs involved in binding phorbol ester in the PKC domains. Since phosphatidylserine is a common ligand, we expect its binding site to be located in regions where the structures of the Raf-1 and PKC domains are similar. The structure of the Raf-1 CRD represents an example of this family of domains that does not bind diacylglycerol and provides a framework for investigating its interactions with other molecules.
+The line below this paragraph, {{ABSTRACT_PUBMED_8710867}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8710867 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8710867}}
 ==About this Structure==
-FAR 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=1FAR OCA].
+FAR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAR OCA].
 ==Reference==
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 [[Category: Transferase]]
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