2jdv

Structure of PKA-PKB chimera complexed with A-443654Structure of PKA-PKB chimera complexed with A-443654

Structural highlights 2jdv is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NonStd Res: , Related: 1kmu, 1kmw, 1q24, 1q61, 1q62, 1q8t, 1q8u, 1q8w, 1smh, 1stc, 1sve, 1svg, 1svh, 1szm, 1veb, 1xh4, 1xh5, 1xh6, 1xh7, 1xh8, 1xh9, 1xha, 1ydr, 1yds, 1ydt, 2c1a, 2c1b, 2f7e, 2gfc, 2gnf, 2gng, 2gnh, 2gni, 2gnj, 2gnl, 1cmk, 2jdo, 2jdr, 2jds, 2jdt Activity: cAMP-dependent protein kinase, with EC number 2.7.11.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IPKA_HUMAN] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Although the crystal structure of the anti-cancer target protein kinase B (PKBbeta/Akt-2) has been useful in guiding inhibitor design, the closely related kinase PKA has generally been used as a structural mimic due to its facile crystallization with a range of ligands. The use of PKB-inhibitor crystallography would bring important benefits, including a more rigorous understanding of factors dictating PKA/PKB selectivity, and the opportunity to validate the utility of PKA-based surrogates. We present a "back-soaking" method for obtaining PKBbeta-ligand crystal structures, and provide a structural comparison of inhibitor binding to PKB, PKA, and PKA-PKB chimera. One inhibitor presented here exhibits no PKB/PKA selectivity, and the compound adopts a similar binding mode in all three systems. By contrast, the PKB-selective inhibitor A-443654 adopts a conformation in PKB and PKA-PKB that differs from that with PKA. We provide a structural explanation for this difference, and highlight the ability of PKA-PKB to mimic the true PKB binding mode in this case. A structural comparison of inhibitor binding to PKB, PKA and PKA-PKB chimera.,Davies TG, Verdonk ML, Graham B, Saalau-Bethell S, Hamlett CC, McHardy T, Collins I, Garrett MD, Workman P, Woodhead SJ, Jhoti H, Barford D J Mol Biol. 2007 Mar 30;367(3):882-94. Epub 2007 Jan 9. PMID:17275837 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CAMP-dependent protein kinase

spinqualitylabelsall models 2jdv, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image