1a38: Difference between revisions

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[[Image:1a38.jpg|left|200px]]
[[Image:1a38.jpg|left|200px]]


{{Structure
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{{STRUCTURE_1a38| PDB=1a38  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a38 OCA], [http://www.ebi.ac.uk/pdbsum/1a38 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a38 RCSB]</span>
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'''14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE'''
'''14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE'''
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[[Category: Pohl, J.]]
[[Category: Pohl, J.]]
[[Category: Wang, B.]]
[[Category: Wang, B.]]
[[Category: complex (signal transduction/peptide)]]
[[Category: Signal transduction]]
[[Category: signal transduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:44:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:32:14 2008''

Revision as of 09:44, 2 May 2008

File:1a38.jpg

Template:STRUCTURE 1a38

14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE


OverviewOverview

14-3-3 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.

About this StructureAbout this Structure

1A38 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 Page seeded by OCA on Fri May 2 09:44:33 2008

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