1daj
From Proteopedia
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COMPARISON OF TERNARY COMPLEXES OF PNEUMOCYSTIS CARINII AND WILD TYPE HUMAN DIHYDROFOLATE REDUCTASE WITH COENZYME NADPH AND A NOVEL CLASSICAL ANTITUMOR FURO[2,3D]PYRIMIDINE ANTIFOLATE
Overview
The novel furopyrimidine, N-(4-{N-[(2,4-diaminofuro[2,3-d]pyrimidin-5-yl)methyl]methylamino}benzoyl), -L- glutamate (MTXO), a classical antifolate with antitumor activity, comparable to that of methotrexate (MTX), has been studied as, inhibitor-cofactor ternary crystal complexes with wild-type Pneumocystis, carinii (pc) and recombinant human wild-type dihydrofolate reductase, (hDHFR). These structural data provide the first direct comparison of the, binding interactions of the same antifolate inhibitor in the active site, for pc and human DHFR. The human ternary DHFR complex crystallizes in the, rhombohedral space group R3 and is isomorphous to the ternary complex, reported for a gamma-tetrazole methotrexate analogue, MTXT. The pcDHFR, complex crystallizes in the monoclinic space group ... [(full description)]
About this Structure
1DAJ is a [Single protein] structure of sequence from [Pneumocystis carinii] with NDP and MOT as [ligands]. Active as [[1]], with EC number [1.5.1.3]. Full crystallographic information is available from [OCA].
Reference
Comparison of ternary complexes of Pneumocystis carinii and wild-type human dihydrofolate reductase with coenzyme NADPH and a novel classical antitumor furo[2,3-d]pyrimidine antifolate., Cody V, Galitsky N, Luft JR, Pangborn W, Gangjee A, Devraj R, Queener SF, Blakley RL, Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):638-49. PMID:15299851
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