1qja: Difference between revisions

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[[Image:1qja.jpg|left|200px]]
{{Seed}}
[[Image:1qja.png|left|200px]]


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{{STRUCTURE_1qja|  PDB=1qja  |  SCENE=  }}  
{{STRUCTURE_1qja|  PDB=1qja  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_10488331}}


==About this Structure==
==About this Structure==
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[[Category: Phosphopeptide]]
[[Category: Phosphopeptide]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:45:21 2008''

Revision as of 21:45, 27 July 2008

File:1qja.png

Template:STRUCTURE 1qja

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

Template:ABSTRACT PUBMED 10488331

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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