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1azs

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{{STRUCTURE_1azs| PDB=1azs | SCENE= }}
{{STRUCTURE_1azs| PDB=1azs | SCENE= }}
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'''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE'''
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===COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 9417641 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9417641}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 14:55, 30 June 2008

Image:1azs.png

Template:STRUCTURE 1azs

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

Template:ABSTRACT PUBMED 9417641

About this Structure

1AZS is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus. 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

Page seeded by OCA on Mon Jun 30 17:55:53 2008

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