1qjb: Difference between revisions

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[[Image:1qjb.gif|left|200px]]
[[Image:1qjb.gif|left|200px]]


{{Structure
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'''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)'''
'''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)'''
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==About this Structure==
==About this Structure==
1QJB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 14PS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJB OCA].  
1QJB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=14ps 14ps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJB OCA].  


==Reference==
==Reference==
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[[Category: Yaffe, M B.]]
[[Category: Yaffe, M B.]]
[[Category: 14-3-3]]
[[Category: 14-3-3]]
[[Category: complex (peptide)]]
[[Category: Phosphopeptide]]
[[Category: phosphopeptide]]
[[Category: Signal transducti]]
[[Category: signal transducti]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:20:37 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:14:25 2008''

Revision as of 06:20, 3 May 2008

File:1qjb.gif

Template:STRUCTURE 1qjb

14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)


OverviewOverview

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 StructureAbout this Structure

1QJB is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 14ps. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 06:20:37 2008

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