1cf1
From Proteopedia
(New page: 200px<br /><applet load="1cf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cf1, resolution 2.8Å" /> '''ARRESTIN FROM BOVINE ...) |
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| - | [[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size=" | + | [[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cf1, resolution 2.8Å" /> | caption="1cf1, resolution 2.8Å" /> | ||
'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br /> | '''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | G protein-coupled signaling is utilized by a wide variety of eukaryotes | + | G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1CF1 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:// | + | 1CF1 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=1CF1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gurevich, V | + | [[Category: Gurevich, V V.]] |
| - | [[Category: Hirsch, J | + | [[Category: Hirsch, J A.]] |
[[Category: Schubert, C.]] | [[Category: Schubert, C.]] | ||
| - | [[Category: Sigler, P | + | [[Category: Sigler, P B.]] |
[[Category: binding to acticated and phosphorylated rhodopsin]] | [[Category: binding to acticated and phosphorylated rhodopsin]] | ||
[[Category: desensitisation of the visual transduction cascade]] | [[Category: desensitisation of the visual transduction cascade]] | ||
[[Category: visual arrestin]] | [[Category: visual arrestin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:28 2008'' |
Revision as of 10:05, 21 February 2008
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ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Overview
G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding.
About this Structure
1CF1 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation., Hirsch JA, Schubert C, Gurevich VV, Sigler PB, Cell. 1999 Apr 16;97(2):257-69. PMID:10219246
Page seeded by OCA on Thu Feb 21 12:05:28 2008
