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 with CMP as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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

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