1cf1: Difference between revisions

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[[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1cf1, resolution 2.8Å" />

'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA].

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==

Line 13:

[[Category: Bos taurus]]

[[Category: Single protein]]

[[Category: Gurevich, V.V.]]

[[Category: Gurevich, V V.]]

[[Category: Hirsch, J.A.]]

[[Category: Hirsch, J A.]]

[[Category: Schubert, C.]]

[[Category: Sigler, P.B.]]

[[Category: Sigler, P B.]]

[[Category: binding to acticated and phosphorylated rhodopsin]]

[[Category: desensitisation of the visual transduction cascade]]

[[Category: visual arrestin]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cf1.gif|left|200px]]<br /><applet load="1cf1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cf1, resolution 2.8&Aring;" />
 '''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''<br />
 ==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.
+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==
-CF1 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA].
+CF1 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==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Gurevich, V.V.]]
+[[Category: Gurevich, V V.]]
-[[Category: Hirsch, J.A.]]
+[[Category: Hirsch, J A.]]
 [[Category: Schubert, C.]]
-[[Category: Sigler, P.B.]]
+[[Category: Sigler, P B.]]
 [[Category: binding to acticated and phosphorylated rhodopsin]]
 [[Category: desensitisation of the visual transduction cascade]]
 [[Category: visual arrestin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:24:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:28 2008''