5es1 | pdb_00005es1

CRYSTAL STRUCTURE OF MICROTUBULE AFFINITY-REGULATING KINASE 4 CATALYTIC DOMAIN IN COMPLEX WITH A PYRAZOLOPYRIMIDINE INHIBITOR

spinqualitylabelsall models 5es1, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5es1 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 2.8Å Ligands: 5RC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MARK4_HUMAN Publication Abstract from PubMed Microtubule-associated protein/microtubule affinity-regulating kinase 4 (MARK4) is a serine/threonine kinase involved in the phosphorylation of MAP proteins that regulate microtubule dynamics. Abnormal activity of MARK4 has been proposed to contribute to neurofibrillary tangle formation in Alzheimer's disease. The crystal structure of the catalytic and ubiquitin-associated domains of MARK4 with a potent pyrazolopyrimidine inhibitor has been determined to 2.8 A resolution with an Rwork of 22.8%. The overall structure of MARK4 is similar to those of the other known MARK isoforms. The inhibitor is located in the ATP-binding site, with the pyrazolopyrimidine group interacting with the inter-lobe hinge region while the aminocyclohexane moiety interacts with the catalytic loop and the DFG motif, forcing the activation loop out of the ATP-binding pocket. Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor.,Sack JS, Gao M, Kiefer SE, Myers JE Jr, Newitt JA, Wu S, Yan C Acta Crystallogr F Struct Biol Commun. 2016 Feb;72(Pt 2):129-34. doi:, 10.1107/S2053230X15024747. Epub 2016 Jan 22. PMID:26841763 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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