Cloning, purification, crystallization and preliminary X-ray analysis of the catalytic domain of human receptor-like protein tyrosine phosphatase γ in three different crystal forms

被引：3

作者：

Kish, Kevin ^{[1
]}

McDonnell, Patricia A. ^{[1
]}

Goldfarb, Valentina ^{[1
]}

Gao, Mian ^{[1
]}

Metzler, William J. ^{[1
]}

Langley, David R. ^{[1
]}

Bryson, James W. ^{[1
]}

Kiefer, Susan E. ^{[1
]}

Carpenter, Brian ^{[1
]}

Kostich, Walter A. ^{[1
]}

Westphal, Ryan S. ^{[1
]}

Sheriff, Steven ^{[1
]}

机构：

[1] Bristol Myers Squibb Res & Dev, Princeton, NJ 08543 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

关键词：

INHIBITORS; KINASE;

D O I：

10.1107/S1744309111017209

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein tyrosine phosphatase gamma is a membrane-bound receptor and is designated RPTP gamma. RPTP gamma and two mutants, RPTP gamma (V948I, S970T) and RPTP gamma (C858S, S970T), were recombinantly expressed and purified for X-ray crystallographic studies. The purified enzymes were crystallized using the hanging-drop vapor-diffusion method. Crystallographic data were obtained from several different crystal forms in the absence and the presence of inhibitor. In this paper, a description is given of how three different crystal forms were obtained that were used with various ligands. An orthorhombic crystal form and a trigonal crystal form were obtained both with and without ligand, and a monoclinic crystal form was only obtained in the presence of a particularly elaborated inhibitor.

引用

页码：768 / 774

页数：7