1a37: Difference between revisions

Revision as of 15:54, 30 June 2008

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File:1a37.png

Template:STRUCTURE 1a37

14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE

Template:ABSTRACT PUBMED 9632691

About this StructureAbout this Structure

1A37 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove., Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC, J Biol Chem. 1998 Jun 26;273(26):16305-10. PMID:9632691

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OCA

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-'''14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE'''
+===14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE===
-==Overview==
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--3-3 proteins bind a variety of molecules involved in signal transduction, cell cycle regulation and apoptosis. 14-3-3 binds ligands such as Raf-1 kinase and Bad by recognizing the phosphorylated consensus motif, RSXpSXP, but must bind unphosphorylated ligands, such as glycoprotein Ib and Pseudomonas aeruginosa exoenzyme S, via a different motif. Here we report the crystal structures of the zeta isoform of 14-3-3 in complex with two peptide ligands: a Raf-derived phosphopeptide (pS-Raf-259, LSQRQRSTpSTPNVHMV) and an unphosphorylated peptide derived from phage display (R18, PHCVPRDLSWLDLEANMCLP) that inhibits binding of exoenzyme S and Raf-1. The two peptides bind within a conserved amphipathic groove on the surface of 14-3-3 at overlapping but distinct sites. The phosphoserine of pS-Raf-259 engages a cluster of basic residues (Lys49, Arg56, Arg60, and Arg127), whereas R18 binds via the amphipathic sequence, WLDLE, with its two acidic groups coordinating the same basic cluster. 14-3-3 is dimeric, and its two peptide-binding grooves are arranged in an antiparallel fashion, 30 A apart. The ability of each groove to bind different peptide motifs suggests how 14-3-3 can act in signal transduction by inducing either homodimer or heterodimer formation in its target proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_9632691}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9632691}}
 ==About this Structure==
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 [[Category: Wang, B.]]
 [[Category: Signal transduction]]
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