3hc8 | pdb_00003hc8

Investigation of Aminopyridiopyrazinones as PDE5 Inhibitors: Evaluation of Modifications to the Central Ring System.

spinqualitylabelsall models 3hc8, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hc8 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, PD4, ZN Related: 2h40, 2h42, 2h44, 3bjc, 1uho, 2chm, 3hdz Gene: PDE5A, PDE5 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PDE5A_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. 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 Efforts to improve the potency and physical properties of the aminopyridiopyrazinone class of PDE5 inhibitors through modification of the core ring system are described. Five new ring systems are evaluated and features that impart improved potency and improved solubility are delineated. Investigation of aminopyridiopyrazinones as PDE5 inhibitors: Evaluation of modifications to the central ring system.,Hughes RO, Walker JK, Cubbage JW, Fobian YM, Rogier DJ, Heasley SE, Blevis-Bal RM, Benson AG, Owen DR, Jacobsen EJ, Freskos JN, Molyneaux JM, Brown DL, Stallings WC, Acker BA, Maddux TM, Tollefson MB, Williams JM, Moon JB, Mischke BV, Rumsey JM, Zheng Y, Macinnes A, Bond BR, Yu Y Bioorg Med Chem Lett. 2009 Aug 1;19(15):4092-6. Epub 2009 Jun 6. PMID:19539468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphodiesterase 3D structures

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