1qjb
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(New page: 200px<br /> <applet load="1qjb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qjb, resolution 2.0Å" /> '''14-3-3 ZETA/PHOSPHOP...)
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Revision as of 16:47, 12 November 2007
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14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)
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
1QJB is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 14PS. 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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