CAMP-dependent protein kinase
From Proteopedia
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In the absence of cAMP, PKA is an inactive tetramer with 2 catalytic subunits and 2 regulatory subunits. The regulatory subunit contains inhibitory region, two cAMP-binding domains and a C-terminal dimerization domain. The catalytic subunit contains an ATP-binding domain and a regulatory subunit binding domain. | In the absence of cAMP, PKA is an inactive tetramer with 2 catalytic subunits and 2 regulatory subunits. The regulatory subunit contains inhibitory region, two cAMP-binding domains and a C-terminal dimerization domain. The catalytic subunit contains an ATP-binding domain and a regulatory subunit binding domain. | ||
| - | *<scene name='46/468128/Cv/ | + | *<scene name='46/468128/Cv/6'>cAMP-binding site of catalytic subunit</scene> ([[4ntt]]).<ref>PMID:25077557</ref> |
| - | *<scene name='46/468128/Cv/ | + | *<scene name='46/468128/Cv/7'>Bovine PKA I-alpha ATP-binding pocket</scene> ([[4jv4]]).<ref>PMID:23978166</ref> |
</StructureSection> | </StructureSection> | ||
==3D structures of cAMP-dependent protein kinase== | ==3D structures of cAMP-dependent protein kinase== | ||
Revision as of 12:31, 10 January 2019
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3D structures of cAMP-dependent protein kinase
Updated on 10-January-2019
References
- ↑ Bastidas AC, Wu J, Taylor SS. Molecular Features of Product Release for the PKA Catalytic Cycle. Biochemistry. 2014 Aug 8. PMID:25077557 doi:http://dx.doi.org/10.1021/bi500684c
- ↑ Brown SH, Cheng CY, Saldanha SA, Wu J, Cottam HB, Sankaran B, Taylor SS. Implementing Fluorescence Anisotropy Screening and Crystallographic Analysis to Define PKA Isoform-Selective Activation by cAMP Analogs. ACS Chem Biol. 2013 Sep 10. PMID:23978166 doi:10.1021/cb400247t
