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1rgs

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{{STRUCTURE_1rgs| PDB=1rgs | SCENE= }}
{{STRUCTURE_1rgs| PDB=1rgs | SCENE= }}
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'''REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE'''
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===REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7638597 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7638597}}
==About this Structure==
==About this Structure==
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[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
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Revision as of 14:13, 27 July 2008

Template:STRUCTURE 1rgs

REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE

Template:ABSTRACT PUBMED 7638597

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

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