1u7e

From Proteopedia

Revision as of 01:46, 21 November 2007

The crystal structure of a Protein Kinase A complex

Overview

The 2.0-angstrom structure of the cyclic adenosine monophosphate, (cAMP)-dependent protein kinase (PKA) catalytic subunit bound to a, deletion mutant of a regulatory subunit (RIalpha) defines a previously, unidentified extended interface. The complex provides a molecular, mechanism for inhibition of PKA and suggests how cAMP binding leads to, activation. The interface defines the large lobe of the catalytic subunit, as a stable scaffold where Tyr247 in the G helix and Trp196 in the, phosphorylated activation loop serve as anchor points for binding RIalpha., These residues compete with cAMP for the phosphate binding cassette in, RIalpha. In contrast to the catalytic subunit, RIalpha undergoes major, conformational changes when the complex is compared with cAMP-bound, RIalpha. The inhibitor sequence docks to the active site, whereas the, linker, also disordered in free RIalpha, folds across the extended, interface. The beta barrel of cAMP binding domain A, which is the docking, site for cAMP, remains largely intact in the complex, whereas the helical, subdomain undergoes major reorganization.

About this Structure

1U7E is a Protein complex structure of sequences from Bos taurus and Mus musculus with MN and ANP as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA., Kim C, Xuong NH, Taylor SS, Science. 2005 Feb 4;307(5710):690-6. PMID:15692043

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