1z23: Difference between revisions

Revision as of 12:15, 28 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:1z23.png

Template:STRUCTURE 1z23

The serine-rich domain from Crk-associated substrate (p130Cas)The serine-rich domain from Crk-associated substrate (p130Cas)

Template:ABSTRACT PUBMED 15795225

About this StructureAbout this Structure

1Z23 is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

ReferenceReference

The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle., Briknarova K, Nasertorabi F, Havert ML, Eggleston E, Hoyt DW, Li C, Olson AJ, Vuori K, Ely KR, J Biol Chem. 2005 Jun 10;280(23):21908-14. Epub 2005 Mar 28. PMID:15795225

Page seeded by OCA on Mon Jul 28 12:15:47 2008

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

OCA

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-'''The serine-rich domain from Crk-associated substrate (p130Cas)'''
+===The serine-rich domain from Crk-associated substrate (p130Cas)===
-==Overview==
+<!--
-p130(cas) (Crk-associated substrate) is a docking protein that is involved in assembly of focal adhesions and concomitant cellular signaling. It plays a role in physiological regulation of cell adhesion, migration, survival, and proliferation, as well as in oncogenic transformation. The molecule consists of multiple protein-protein interaction motifs, including a serine-rich region that is positioned between Crk and Src-binding sites. This study reports the first structure of a functional domain of Cas. The solution structure of the serine-rich region has been determined by NMR spectroscopy, demonstrating that this is a stable domain that folds as a four-helix bundle, a protein-interaction motif. The serine-rich region bears strong structural similarity to four-helix bundles found in other adhesion components like focal adhesion kinase, alpha-catenin, or vinculin. Potential sites for phosphorylation and interaction with the 14-3-3 family of cellular regulators are identified in the domain and characterized by site-directed mutagenesis and binding assays. Mapping the degree of amino acid conservation onto the molecular surface reveals a patch of invariant residues near the C terminus of the bundle, which may represent a previously unidentified site for protein interaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_15795225}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15795225 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15795225}}
 ==About this Structure==
-Z23 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z23 OCA].
+Z23 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z23 OCA].
 ==Reference==
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 [[Category: Vuori, K.]]
 [[Category: Four-helix bundle]]
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