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Article

Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations.

The Journal of biological chemistry - 14 May 2010

McNicholl E Tyler, Das Rahul, SilDas Soumita, Taylor Susan S, Melacini Giuseppe

Abstract excerpt

Protein kinase A (PKA) is the main receptor for the universal cAMP second messenger. PKA is a tetramer with two catalytic (C) and two regulatory (R) subunits, each including two tandem cAMP binding domains, i.e. CBD-A and -B. Structural investigations of RIalpha have revealed that although CBD-A plays a pivotal role in the cAMP-dependent inhibition of C, the main function of CBD-B is to regulate the access of...

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Identifiers

PMID: 20202931
DOI: 10.1074/jbc.M110.105783
PMCID: PMC2865341

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