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3OCP

Crystal structure of cAMP bound cGMP-dependent protein kinase(92-227)

Summary for 3OCP
Entry DOI10.2210/pdb3ocp/pdb
Related3OD0 3OGJ
DescriptorPRKG1 protein, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
Functional Keywordsserine/threonine kinase, tf2i and irag, transferase
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight31872.77
Authors
Kim, J.J.,Huang, G.,Kwon, T.K.,Zwart, P.,Headd, J.,Kim, C. (deposition date: 2010-08-10, release date: 2011-05-11, Last modification date: 2023-09-06)
Primary citationKim, J.J.,Casteel, D.E.,Huang, G.,Kwon, T.H.,Ren, R.K.,Zwart, P.,Headd, J.J.,Brown, N.G.,Chow, D.C.,Palzkill, T.,Kim, C.
Co-Crystal Structures of PKG Ibeta (92-227) with cGMP and cAMP Reveal the Molecular Details of Cyclic-Nucleotide Binding
Plos One, 6:e18413-e18413, 2011
Cited by
PubMed Abstract: Cyclic GMP-dependent protein kinases (PKGs) are central mediators of the NO-cGMP signaling pathway and phosphorylate downstream substrates that are crucial for regulating smooth muscle tone, platelet activation, nociception and memory formation. As one of the main receptors for cGMP, PKGs mediate most of the effects of cGMP elevating drugs, such as nitric oxide-releasing agents and phosphodiesterase inhibitors which are used for the treatment of angina pectoris and erectile dysfunction, respectively.
PubMed: 21526164
DOI: 10.1371/journal.pone.0018413
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.49 Å)
Structure validation

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