3zm9

The mechanism of allosteric coupling in choline kinase a1 revealed by a rationally designed inhibitor

spinqualitylabelsall models 3zm9, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zm9 is a 2 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 1.9Å Ligands: QMQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHKA_HUMAN Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline. Publication Abstract from PubMed Applying a CHOK hold: Combined experimental and computational studies of the binding mode of a rationally designed inhibitor of the dimeric choline kinase alpha1 (CHOKalpha1) explain the molecular mechanism of negative cooperativity and how the monomers are connected. The results give insight into how the symmetry of the dimer can be partially conserved despite a lack of conservation in the static crystal structures. The Mechanism of Allosteric Coupling in Choline Kinase alpha1 Revealed by the Action of a Rationally Designed Inhibitor.,Sahun-Roncero M, Rubio-Ruiz B, Saladino G, Conejo-Garcia A, Espinosa A, Velazquez-Campoy A, Gervasio FL, Entrena A, Hurtado-Guerrero R Angew Chem Int Ed Engl. 2013 Feb 25. doi: 10.1002/anie.201209660. PMID:23441033 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Choline kinase 3D structures

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