7lcb | pdb_00007lcb

C1B domain of Protein kinase C in complex with prostratin and phosphatidylcholine

spinqualitylabelsall models 7lcb, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7lcb is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: XP5, XYV, ZN Activity: Protein kinase C, with EC number 2.7.11.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A140UHX0_RAT] Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression.[PIRNR:PIRNR000551] Publication Abstract from PubMed Diacylglycerol (DAG) is a versatile lipid whose 1,2-sn-stereoisomer serves both as second messenger in signal transduction pathways that control vital cellular processes, and as metabolic precursor for downstream signaling lipids such as phosphatidic acid. Effector proteins translocate to available DAG pools in the membranes by using conserved homology 1 (C1) domains as DAG-sensing modules. Yet, how C1 domains recognize and capture DAG in the complex environment of a biological membrane has remained unresolved for the 40 years since the discovery of Protein Kinase C (PKC) as the first member of the DAG effector cohort. Herein, we report the high-resolution crystal structures of a C1 domain (C1B from PKCdelta) complexed to DAG and to each of four potent PKC agonists that produce different biological readouts and that command intense therapeutic interest. This structural information details the mechanisms of stereospecific recognition of DAG by the C1 domains, the functional properties of the lipid-binding site, and the identities of the key residues required for the recognition and capture of DAG and exogenous agonists. Moreover, the structures of the five C1 domain complexes provide the high-resolution guides for the design of agents that modulate the activities of DAG effector proteins. Structural anatomy of Protein Kinase C C1 domain interactions with diacylglycerol and other agonists.,Katti SS, Krieger IV, Ann J, Lee J, Sacchettini JC, Igumenova TI Nat Commun. 2022 May 16;13(1):2695. doi: 10.1038/s41467-022-30389-2. PMID:35577811 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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