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1a4o
From Proteopedia
(New page: 200px<br /><applet load="1a4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4o, resolution 2.8Å" /> '''14-3-3 PROTEIN ZETA I...) |
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| - | [[Image:1a4o.gif|left|200px]]<br /><applet load="1a4o" size=" | + | [[Image:1a4o.gif|left|200px]]<br /><applet load="1a4o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a4o, resolution 2.8Å" /> | caption="1a4o, resolution 2.8Å" /> | ||
'''14-3-3 PROTEIN ZETA ISOFORM'''<br /> | '''14-3-3 PROTEIN ZETA ISOFORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 14-3-3 family of proteins have recently been identified as regulatory | + | 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== | ==About this Structure== | ||
| - | 1A4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1A4O is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bienkowska, J.]] | [[Category: Bienkowska, J.]] | ||
| - | [[Category: Collier, R | + | [[Category: Collier, R J.]] |
[[Category: Fu, H.]] | [[Category: Fu, H.]] | ||
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
[[Category: Liu, D.]] | [[Category: Liu, D.]] | ||
[[Category: Petosa, C.]] | [[Category: Petosa, C.]] | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:50 2008'' |
Revision as of 09:40, 21 February 2008
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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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