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1rl3
From Proteopedia
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Crystal structure of cAMP-free R1a subunit of PKA
Overview
In eukaryotes the primary target for cAMP, a ubiquitous second messenger, is cAMP-dependent protein kinase (PKA). Understanding how binding and, release of cAMP changes the cAMP binding domains and then triggers, long-range allosteric responses is an important challenge. This, conformational switching requires structure solutions of cAMP binding, domains in cAMP-bound and cAMP-free states. We describe for the first time, a crystal structure of the cAMP binding domains of PKA type Ialpha, regulatory subunit where site A is occupied by cGMP and site B is, unoccupied. The structure reveals that the carboxyl terminus of domain B, serves as a hydrophobic cap, locking the cyclic nucleotide via its adenine, ring into the beta-barrel. In the absence of cAMP, the "cap" is released, via an extension of the C-terminal helix. This simple hinge mechanism for, binding and release of cAMP also provides a mechanism for allosteric, communication between sites A and B.
About this Structure
1RL3 is a Single protein structure of sequence from Bos taurus with PCG and GOL as ligands. Full crystallographic information is available from OCA.
Reference
RIalpha subunit of PKA: a cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B., Wu J, Brown S, Xuong NH, Taylor SS, Structure. 2004 Jun;12(6):1057-65. PMID:15274925
Page seeded by OCA on Wed Nov 21 01:40:43 2007
