1RGS

REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE

Summary for 1RGS

• Entry DOI: 10.2210/pdb1rgs/pdb
• Descriptor: CAMP DEPENDENT PROTEIN KINASE, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (2 entities in total)
• Functional Keywords: regulatory subunit, kinase
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 33152.27

Authors

Su, Y.,Dostmann, W.R.G.,Herberg, F.W.,Durick, K.,Xuong, N.-H.,Ten Eyck, L.,Taylor, S.S.,Varughese, K.I. (deposition date: 1995-06-21, release date: 1996-12-07, Last modification date: 2024-02-14)

Primary citation

Su, Y.,Dostmann, W.R.,Herberg, F.W.,Durick, K.,Xuong, N.H.,Ten Eyck, L.,Taylor, S.S.,Varughese, K.I.
Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains.
Science, 269:807-813, 1995

PubMed Abstract: 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.

PubMed: 7638597

Experimental method

X-RAY DIFFRACTION (2.8 Å)