1DRF

CRYSTAL STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE

1DRF の概要

• エントリーDOI: 10.2210/pdb1drf/pdb
• 分子名称: DIHYDROFOLATE REDUCTASE, SULFATE ION, FOLIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase (ch-nh(d)-nad or nadp(a))
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21983.05

構造登録者

Oefner, C.,D'Arcy, A.,Winkler, F.K. (登録日: 1990-08-09, 公開日: 1992-01-15, 最終更新日: 2024-02-07)

主引用文献

Oefner, C.,D'Arcy, A.,Winkler, F.K.
Crystal structure of human dihydrofolate reductase complexed with folate.
Eur.J.Biochem., 174:377-385, 1988

PubMed Abstract: The crystal structure of recombinant human dihydrofolate reductase with folate bound in the active site has been determined and the structural model refined at 0.2-nm resolution. Preliminary studies of the binding of the inhibitors methotrexate and trimethoprim to the human apoenzyme have been performed at 0.35-nm resolution. The conformations of the chemically very similar ligands folate and methotrexate, one a substrate the other a potent inhibitor, differ substantially in that their pteridine rings are in inverse orientations relative to their p-aminobenzoyl-L-glutamate moieties. Methotrexate binding is similar to that previously observed in two bacterial enzymes but is quite different from that observed in the enzyme from a mouse lymphoma cell line [Stammers et al. (1987) FEBS Lett. 218, 178-184]. The geometry of the polypeptide chain around the folate binding site in the human enzyme is not consistent with conclusions previously drawn with regard to the species selectivity of the inhibitor trimethoprim [Matthews et al. (1985) J. Biol. Chem. 260, 392-399].

PubMed: 3383852
DOI: 10.1111/j.1432-1033.1988.tb14108.x

実験手法

X-RAY DIFFRACTION (2 Å)