1a4o: Difference between revisions

Revision as of 16:07, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1a4o.png

Template:STRUCTURE 1a4o

14-3-3 PROTEIN ZETA ISOFORM14-3-3 PROTEIN ZETA ISOFORM

Template:ABSTRACT PUBMED 7603574

About this StructureAbout this Structure

1A4O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the zeta isoform of the 14-3-3 protein., Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R, Nature. 1995 Jul 13;376(6536):191-4. PMID:7603574

Page seeded by OCA on Mon Jun 30 16:07:05 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1a4o.gif|left|200px]]
+{{Seed}}
+[[Image:1a4o.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1a4o|  PDB=1a4o  |  SCENE=  }}
-'''14-3-3 PROTEIN ZETA ISOFORM'''
+===14-3-3 PROTEIN ZETA ISOFORM===
-==Overview==
+<!--
-The 14-3-3 family of proteins have recently been identified as regulatory elements in intracellular signalling pathways: 14-3-3 proteins bind to oncogene and proto-oncogene products, including c-Raf-1 (refs 2-5), c-Bcr (ref. 6) and polyomavirus middle-T antigen; overexpression of 14-3-3 activates Raf kinase in yeast and induces meiotic maturation in Xenopus oocytes. Here we report the crystal structure of the major isoform of mammalian 14-3-3 proteins at 2.9 A resolution. Each subunit of the dimeric protein consists of a bundle of nine antiparallel helices that form a palisade around an amphipathic groove. The groove is large enough to accommodate a tenth helix, and we propose that binding to an amphipathic helix represents a general mechanism for the interaction of 14-3-3 with diverse cellular proteins. The residues in the dimer interface and the putative ligand-binding surface are invariant among vertebrates, yeast and plants, suggesting a conservation of structure and function throughout the 14-3-3 family.
+The line below this paragraph, {{ABSTRACT_PUBMED_7603574}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7603574 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7603574}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Petosa, C.]]
 [[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:48:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:07:05 2008''