1a38: Difference between revisions

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


{{Structure
==14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE==
|PDB= 1a38 |SIZE=350|CAPTION= <scene name='initialview01'>1a38</scene>, resolution 3.35&Aring;
<StructureSection load='1a38' size='340' side='right'caption='[[1a38]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1a38]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A38 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a38 OCA], [https://pdbe.org/1a38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a38 RCSB], [https://www.ebi.ac.uk/pdbsum/1a38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a38 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|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>
[https://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a38_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a38 ConSurf].
<div style="clear:both"></div>


'''14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE'''
==See Also==
 
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1A38 is a [[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==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9632691 9632691]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fu, H.]]
[[Category: Fu H]]
[[Category: Liddington, R C.]]
[[Category: Liddington RC]]
[[Category: Masters, S C.]]
[[Category: Masters SC]]
[[Category: Petosa, C.]]
[[Category: Petosa C]]
[[Category: Pohl, J.]]
[[Category: Pohl J]]
[[Category: Wang, B.]]
[[Category: Wang B]]
[[Category: complex (signal transduction/peptide)]]
[[Category: signal transduction]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:32:14 2008''

Latest revision as of 09:27, 7 February 2024

14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE

Structural highlights

1a38 is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.35Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

1433Z_BOVIN Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Tanji M, Horwitz R, Rosenfeld G, Waymire JC. Activation of protein kinase C by purified bovine brain 14-3-3: comparison with tyrosine hydroxylase activation. J Neurochem. 1994 Nov;63(5):1908-16. PMID:7931346

1a38, resolution 3.35Å

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