1a4o: Difference between revisions
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[[Image:1a4o.gif|left|200px]] | [[Image:1a4o.gif|left|200px]] | ||
'''14-3-3 PROTEIN ZETA ISOFORM''' | {{Structure | ||
|PDB= 1a4o |SIZE=350|CAPTION= <scene name='initialview01'>1a4o</scene>, resolution 2.8Å | |||
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|LIGAND= | |||
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'''14-3-3 PROTEIN ZETA ISOFORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A4O is a [ | 1A4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4O OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7603574 7603574] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:50 2008'' | ||
Revision as of 07:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
About this Structure
1A4O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
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