3j4r | pdb_00003j4r

Pseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopy

Loading... Status: waiting for Mol* initialization Structural highlights 3j4r is a 5 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 35Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AKA7G_RAT Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane.[UniProtKB:Q9P0M2] Publication Abstract from PubMed Anchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell. Mechanistic understanding of this process is hampered by limited structural information on these macromolecular complexes. A-kinase anchoring proteins (AKAPs) spatially constrain phosphorylation by cAMP-dependent protein kinases (PKA). Electron microscopy and three-dimensional reconstructions of type-II PKA-AKAP18gamma complexes reveal hetero-pentameric assemblies that adopt a range of flexible tripartite configurations. Intrinsically disordered regions within each PKA regulatory subunit impart the molecular plasticity that affords an approximately 16 nanometer radius of motion to the associated catalytic subunits. Manipulating flexibility within the PKA holoenzyme augmented basal and cAMP responsive phosphorylation of AKAP-associated substrates. Cell-based analyses suggest that the catalytic subunit remains within type-II PKA-AKAP18gamma complexes upon cAMP elevation. We propose that the dynamic movement of kinase sub-structures, in concert with the static AKAP-regulatory subunit interface, generates a solid-state signaling microenvironment for substrate phosphorylation. DOI: https://dx.doi.org/10.7554/eLife.01319.001. Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation.,Smith FD, Reichow SL, Esseltine JL, Shi D, Langeberg LK, Scott JD, Gonen T Elife. 2013 Nov 5;2(0). pii: e01319. doi: 10.7554/eLife.01319. PMID:24192038 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also A-kinase anchor protein 3D structures CAMP-dependent protein kinase 3D structures

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