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| {{STRUCTURE_1a38| PDB=1a38 | SCENE= }} | | {{STRUCTURE_1a38| PDB=1a38 | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9632691}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9632691 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9632691}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Wang, B.]] | | [[Category: Wang, B.]] |
| [[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 Mon Jun 30 15:54:25 2008'' |