1azs

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==Overview==
==Overview==
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The crystal structure of a soluble, catalytically active form of adenylyl, cyclase in a complex with its stimulatory heterotrimeric G protein alpha, subunit (Gsalpha) and forskolin was determined to a resolution of 2.3, angstroms. When P-site inhibitors were soaked into native crystals of the, complex, the active site of adenylyl cyclase was located and structural, elements important for substrate recognition and catalysis were, identified. On the basis of these and other structures, a molecular, mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.
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The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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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: FKP]]
[[Category: FKP]]
[[Category: GSP]]
[[Category: GSP]]
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[[Category: signal transducing protein]]
[[Category: signal transducing protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:04 2008''

Revision as of 09:50, 21 February 2008


1azs, resolution 2.3Å

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COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE

Overview

The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.

About this Structure

1AZS is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus with , and as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS., Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR, Science. 1997 Dec 12;278(5345):1907-16. PMID:9417641

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