CAMP-dependent protein kinase

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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.
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*<scene name='46/468128/Cv/3'>cAMP-binding site of catalytic subunit</scene> ([[4ntt]]).
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*<scene name='46/468128/Cv/3'>cAMP-binding site of catalytic subunit</scene> ([[4ntt]]).<ref>PMID:25077557</ref>
</StructureSection>
</StructureSection>
==3D structures of cAMP-dependent protein kinase==
==3D structures of cAMP-dependent protein kinase==
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**[[3j4q]], [[3j4r]] – mPKA + A-kinase anchor protein 18<br />
**[[3j4q]], [[3j4r]] – mPKA + A-kinase anchor protein 18<br />
}}
}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:12, 19 November 2015

PDB ID 1xh6

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3D structures of cAMP-dependent protein kinase

Updated on 19-November-2015

References

  1. 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

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Michal Harel, Alexander Berchansky

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