1qjb: Difference between revisions

Revision as of 14:31, 27 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:1qjb.png

Template:STRUCTURE 1qjb

14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)

Template:ABSTRACT PUBMED 10488331

About this StructureAbout this Structure

1QJB is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 14ps. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding., Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB, Mol Cell. 1999 Aug;4(2):153-66. PMID:10488331

Page seeded by OCA on Sun Jul 27 14:31:07 2008

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

OCA

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-'''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)'''
+===14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)===
-==Overview==
+<!--
-We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery.
+The line below this paragraph, {{ABSTRACT_PUBMED_10488331}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10488331 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10488331}}
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 [[Category: Phosphopeptide]]
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