1jr1
From Proteopedia
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Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid
Overview
The structure of inosine-5'-monophosphate dehydrogenase (IMPDH) in complex with IMP and mycophenolic acid (MPA) has been determined by X-ray diffraction. IMPDH plays a central role in B and T lymphocyte replication. MPA is a potent IMPDH inhibitor and the active metabolite of an immunosuppressive drug recently approved for the treatment of allograft rejection. IMPDH comprises two domains: a core domain, which is an alpha/beta barrel and contains the active site, and a flanking domain. The complex, in combination with mutagenesis and kinetic data, provides a structural basis for understanding the mechanism of IMPDH activity and indicates that MPA inhibits IMPDH by acting as a replacement for the nicotinamide portion of the nicotinamide adenine dinucleotide cofactor and a catalytic water molecule.
About this Structure
1JR1 is a Single protein structure of sequence from Cricetulus griseus with , and as ligands. Active as IMP dehydrogenase, with EC number 1.1.1.205 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid., Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP, Cell. 1996 Jun 14;85(6):921-30. PMID:8681386
Page seeded by OCA on Thu Feb 21 13:25:47 2008
Categories: Cricetulus griseus | IMP dehydrogenase | Single protein | Caron, P R. | Chambers, S P. | Fleming, M A. | Futer, O. | Murcko, M A. | Raybuck, S A. | Sintchak, M D. | Wilson, K P. | IMP | K | MOA | Dehydrogenase | Guanine nucleotide synthesis | Impd | Impdh | Mpa | Mycophenolic acid
