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1a38
From Proteopedia
(New page: 200px<br /><applet load="1a38" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a38, resolution 3.35Å" /> '''14-3-3 PROTEIN ZETA ...) |
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| - | [[Image:1a38.jpg|left|200px]]<br /><applet load="1a38" size=" | + | [[Image:1a38.jpg|left|200px]]<br /><applet load="1a38" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a38, resolution 3.35Å" /> | caption="1a38, resolution 3.35Å" /> | ||
'''14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE'''<br /> | '''14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 14-3-3 proteins bind a variety of molecules involved in signal | + | 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 Structure== | ==About this Structure== | ||
| - | 1A38 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1A38 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A38 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fu, H.]] | [[Category: Fu, H.]] | ||
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
| - | [[Category: Masters, S | + | [[Category: Masters, S C.]] |
[[Category: Petosa, C.]] | [[Category: Petosa, C.]] | ||
[[Category: Pohl, J.]] | [[Category: Pohl, J.]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:20 2008'' |
Revision as of 09:40, 21 February 2008
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14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE
Overview
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 Structure
1A38 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 11:40:20 2008
