1so2
From Proteopedia
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CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 3B In COMPLEX WITH A DIHYDROPYRIDAZINE INHIBITOR
Overview
Phosphodiesterases (PDEs) are enzymes that modulate cyclic nucleotide, signaling and as such are clinical targets for a range of disorders, including congestive heart failure, erectile dysfunction, and, inflammation. The PDE3 family comprises two highly homologous subtypes, expressed in different tissues, and inhibitors of this family have been, shown to increase lipolysis in adipocytes. A specific PDE3B (the, lipocyte-localized subtype) inhibitor would be a very useful tool to, evaluate the effects of PDE3 inhibition on lipolysis and metabolic rate, and might become a novel tool for treatment of obesity. We report here the, three-dimensional structures of the catalytic domain of human PDE3B in, complex with a generic PDE inhibitor and a novel PDE3 selective inhibitor., These structures explain the dual cAMP/cGMP binding capabilities of PDE3, provide the molecular basis for inhibitor specificity, and can supply a, valid platform for the design of improved compounds.
About this Structure
1SO2 is a Single protein structure of sequence from Homo sapiens with MG, HG9 and 666 as ligands. Active as 3',5'-cyclic-nucleotide phosphodiesterase, with EC number 3.1.4.17 Full crystallographic information is available from OCA.
Reference
Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity., Scapin G, Patel SB, Chung C, Varnerin JP, Edmondson SD, Mastracchio A, Parmee ER, Singh SB, Becker JW, Van der Ploeg LH, Tota MR, Biochemistry. 2004 May 25;43(20):6091-100. PMID:15147193
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