1qja

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|PDB= 1qja |SIZE=350|CAPTION= <scene name='initialview01'>1qja</scene>, resolution 2.0&Aring;
|PDB= 1qja |SIZE=350|CAPTION= <scene name='initialview01'>1qja</scene>, resolution 2.0&Aring;
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|LIGAND= <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qja OCA], [http://www.ebi.ac.uk/pdbsum/1qja PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qja RCSB]</span>
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:38:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:14:25 2008''

Revision as of 20:14, 30 March 2008


PDB ID 1qja

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)


Overview

We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery.

About this Structure

1QJA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding., Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB, Mol Cell. 1999 Aug;4(2):153-66. PMID:10488331

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