4daw

Crystal structure of PAK1 kinase domain with the ruthenium phthalimide complex

spinqualitylabelsall models 4daw, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4daw is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 0H2, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAK1_HUMAN Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Publication Abstract from PubMed Better fit, less effort: An easy-to-synthesize ruthenium phthalimide complex (tan-colored carbon atoms in the picture) was designed to bind within the active site of the p21-activated kinase 1 in a novel fashion that differs from that of the previously established staurosporine-inspired metallopyridocarbazoles (gray-colored carbon atoms). The Art of Filling Protein Pockets Efficiently with Octahedral Metal Complexes.,Blanck S, Maksimoska J, Baumeister J, Harms K, Marmorstein R, Meggers E Angew Chem Int Ed Engl. 2012 Mar 1. doi: 10.1002/anie.201108865. PMID:22383326 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase 3D structures

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