A homology model for the human Theta-class glutathione transferase T1-1

被引:0
|
作者
Flanagan, JU
Rossjohn, J
Parker, MW
Board, PG
Chelvanayagam, G [1 ]
机构
[1] Australian Natl Univ, John Curtin Sch Med Res, Canberra, ACT 2601, Australia
[2] St Vincents Inst Med Res, Ian Potter Fdn Prot Crystallog Lab, Melbourne, Vic, Australia
关键词
hGSTT1-1; homology modeling; menaphthyl sulfate; dichloromethane; dehalogenase;
D O I
10.1002/(SICI)1097-0134(19981115)33:3<444::AID-PROT12>3.0.CO;2-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A manual threading approach is used to model the human glutathione transferase T1-1 based on the coordinates of the related Theta class enzyme T2-2, The low level of sequence identity (about 20%), found in the C-terminal extension in conjunction with a relative deletion of about five residues makes this a challenging modeling problem, The C-terminal extension contributes to the active site of the molecule and is thus of particular interest for understanding the molecular mechanism of the enzyme, Manual docking of known substrates and non-substrates has implicated potential candidates for the T1-1 catalytic residues involved in the dehalogenation and epoxide-ring opening activities. These include the conserved Theta class residues Arg 107, Trp 115, and the conserved GSTT1 subclass residue His 176, Also, the residue at position 234 is implicated in the modulation of T1-1 activity with different substrates between species. Proteins 33:444-454, 1998, (C) 1998 Wiley-Liss, Inc.
引用
收藏
页码:444 / 454
页数:11
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