1jsy: Difference between revisions

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

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

caption="1jsy, resolution 2.9Å" />

'''Crystal structure of bovine arrestin-2'''<br />

==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.

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 [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].

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==

Line 13:

[[Category: Bos taurus]]

[[Category: Single protein]]

[[Category: Benovic, J.L.]]

[[Category: Benovic, J L.]]

[[Category: Brenner, C.]]

[[Category: Kim, Y.M.]]

[[Category: Kim, Y M.]]

[[Category: Milano, S.K.]]

[[Category: Milano, S K.]]

[[Category: Pace, H.C.]]

[[Category: Pace, H C.]]

[[Category: beta-arrestins]]

[[Category: desensitization]]

Line 24:

[[Category: nonvisual arrestins]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 18~~:33:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1jsy.gif|left|200px]]<br /><applet load="1jsy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jsy.gif|left|200px]]<br /><applet load="1jsy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jsy, resolution 2.9&Aring;" />
 '''Crystal structure of bovine arrestin-2'''<br />
 ==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.
+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==
-JSY 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].
+JSY 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==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Benovic, J.L.]]
+[[Category: Benovic, J L.]]
 [[Category: Brenner, C.]]
-[[Category: Kim, Y.M.]]
+[[Category: Kim, Y M.]]
-[[Category: Milano, S.K.]]
+[[Category: Milano, S K.]]
-[[Category: Pace, H.C.]]
+[[Category: Pace, H C.]]
 [[Category: beta-arrestins]]
 [[Category: desensitization]]
@@ Line 24: / Line 24: @@
 [[Category: nonvisual arrestins]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:33:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:21 2008''