1jr1

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1jr1, resolution 2.6Å

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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 K, IMP and MOA 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

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