1qjb: Difference between revisions

Revision as of 15:40, 21 February 2008

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 Thu Feb 21 14:40:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1qjb.gif|left|200px]]<br />
+[[Image:1qjb.gif|left|200px]]<br /><applet load="1qjb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1qjb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1qjb, resolution 2.0&Aring;" />
 '''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1)'''<br />
 ==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.
+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==
-QJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 14PS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJB OCA].
+QJB is a [http://en.wikipedia.org/wiki/Single_protein 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].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Budman, J.]]
-[[Category: Cantley, L.C.]]
+[[Category: Cantley, L C.]]
-[[Category: Gamblin, S.J.]]
+[[Category: Gamblin, S J.]]
 [[Category: Rittinger, K.]]
-[[Category: Smerdon, S.J.]]
+[[Category: Smerdon, S J.]]
 [[Category: Volinia, S.]]
 [[Category: Xu, J.]]
-[[Category: Yaffe, M.B.]]
+[[Category: Yaffe, M B.]]
 [[Category: 14-3-3]]
 [[Category: complex (peptide)]]
@@ Line 27: / Line 26: @@
 [[Category: signal transducti]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:53:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:15 2008''