1jsy

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(New page: 200px<br /><applet load="1jsy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jsy, resolution 2.9&Aring;" /> '''Crystal structure of ...)
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caption="1jsy, resolution 2.9&Aring;" />
'''Crystal structure of bovine arrestin-2'''<br />
'''Crystal structure of bovine arrestin-2'''<br />
==Overview==
==Overview==
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Arrestin binding to activated, phosphorylated G protein-coupled receptors, (GPCRs) represents a critical step in regulation of light- and, hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and, terminating signaling events. Using a combination of X-ray, crystallography, molecular modeling, mutagenesis, and binding analysis, we, reveal structural features of arrestin-2 that may enable simultaneous, binding to phosphorylated receptor, SH3 domains, phosphoinositides, and, beta-adaptin. The structure of full-length arrestin-2 thus provides a, uniquely oriented scaffold for assembly of multiple, diverse molecules, involved in GPCR signal transduction.
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Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction.
==About this Structure==
==About this Structure==
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1JSY 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=1JSY OCA].
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1JSY 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=1JSY OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Benovic, J.L.]]
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[[Category: Benovic, J L.]]
[[Category: Brenner, C.]]
[[Category: Brenner, C.]]
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[[Category: Kim, Y.M.]]
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[[Category: Kim, Y M.]]
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[[Category: Milano, S.K.]]
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[[Category: Milano, S K.]]
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[[Category: Pace, H.C.]]
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[[Category: Pace, H C.]]
[[Category: beta-arrestins]]
[[Category: beta-arrestins]]
[[Category: desensitization]]
[[Category: desensitization]]
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[[Category: nonvisual arrestins]]
[[Category: nonvisual arrestins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:33:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:21 2008''

Revision as of 11:26, 21 February 2008


1jsy, resolution 2.9Å

Drag the structure with the mouse to rotate

Crystal structure of bovine arrestin-2

Overview

Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction.

About this Structure

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

Reference

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis., Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL, Biochemistry. 2002 Mar 12;41(10):3321-8. PMID:11876640

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