1azt

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(New page: 200px<br /><applet load="1azt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azt, resolution 2.3&Aring;" /> '''GS-ALPHA COMPLEXED WI...)
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[[Image:1azt.jpg|left|200px]]<br /><applet load="1azt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1azt.jpg|left|200px]]<br /><applet load="1azt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1azt, resolution 2.3&Aring;" />
caption="1azt, resolution 2.3&Aring;" />
'''GS-ALPHA COMPLEXED WITH GTP-GAMMA-S'''<br />
'''GS-ALPHA COMPLEXED WITH GTP-GAMMA-S'''<br />
==Overview==
==Overview==
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The crystal structure of Gsalpha, the heterotrimeric G protein alpha, subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a, complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is, the prototypic member of a family of GTP-binding proteins that regulate, the activities of effectors in a hormone-dependent manner. Comparison of, the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests, that their effector specificity is primarily dictated by the shape of the, binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein, signaling to stimulate the GTPase activity of Gsalpha. The betagamma, binding surface of Gsalpha is largely conserved in sequence and structure, to that of Gialpha, whereas differences in the surface formed by the, carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor, specificity.
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The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding surface of Gsalpha is largely conserved in sequence and structure to that of Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor specificity.
==About this Structure==
==About this Structure==
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1AZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, PO4 and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AZT OCA].
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1AZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZT OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sprang, S.R.]]
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[[Category: Sprang, S R.]]
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[[Category: Tesmer, J.J.G.]]
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[[Category: Tesmer, J J.G.]]
[[Category: GSP]]
[[Category: GSP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: signal transducing protein]]
[[Category: signal transducing protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:14:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:00 2008''

Revision as of 09:50, 21 February 2008


1azt, resolution 2.3Å

Drag the structure with the mouse to rotate

GS-ALPHA COMPLEXED WITH GTP-GAMMA-S

Overview

The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding surface of Gsalpha is largely conserved in sequence and structure to that of Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor specificity.

About this Structure

1AZT is a Single protein structure of sequence from Bos taurus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the adenylyl cyclase activator Gsalpha., Sunahara RK, Tesmer JJ, Gilman AG, Sprang SR, Science. 1997 Dec 12;278(5345):1943-7. PMID:9395396

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