1so2

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{{STRUCTURE_1so2| PDB=1so2 | SCENE= }}
{{STRUCTURE_1so2| PDB=1so2 | SCENE= }}
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'''CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 3B In COMPLEX WITH A DIHYDROPYRIDAZINE INHIBITOR'''
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===CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 3B In COMPLEX WITH A DIHYDROPYRIDAZINE INHIBITOR===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15147193}}
==About this Structure==
==About this Structure==
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[[Category: Varnerin, J P.]]
[[Category: Varnerin, J P.]]
[[Category: Pde3b phosphodiesterase]]
[[Category: Pde3b phosphodiesterase]]
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Revision as of 22:09, 28 July 2008

Image:1so2.png

Template:STRUCTURE 1so2

CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 3B In COMPLEX WITH A DIHYDROPYRIDAZINE INHIBITOR

Template:ABSTRACT PUBMED 15147193

About this Structure

1SO2 is a Single protein structure of sequence from Homo sapiens. 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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