1qja
From Proteopedia
(New page: 200px<br /> <applet load="1qja" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qja, resolution 2.0Å" /> '''14-3-3 ZETA/PHOSPHOP...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qja. | + | [[Image:1qja.jpg|left|200px]]<br /><applet load="1qja" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qja" size=" | + | |
caption="1qja, resolution 2.0Å" /> | caption="1qja, resolution 2.0Å" /> | ||
'''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)'''<br /> | '''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1QJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1QJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJA OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:44:54 2008'' |
Revision as of 14:44, 15 February 2008
|
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
Page seeded by OCA on Fri Feb 15 16:44:54 2008
