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1rgs
From Proteopedia
REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE
Overview
In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.
About this Structure
1RGS is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains., Su Y, Dostmann WR, Herberg FW, Durick K, Xuong NH, Ten Eyck L, Taylor SS, Varughese KI, Science. 1995 Aug 11;269(5225):807-13. PMID:7638597 Page seeded by OCA on Sat May 3 07:28:38 2008
