Crystals of the β-subunit of bovine luteinizing hormone and indicators for the involvement of proteolysis in protein crystallization

被引：6

作者：

McPherson, A ^{[1
]}

Day, J ^{[1
]}

Harris, LJ ^{[1
]}

机构：

[1] Dept Biochem & Mol Biol, Irvine, CA 92697 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S0907444904005025

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The beta-subunit of luteinizing hormone (LH), the subunit responsible for the physiological response, has been crystallized beginning with the intact alphabeta-heterodimeric hormone purified from bovine pituitary glands. The crystals were grown at 310 K in the presence of neutral detergents along with trypsin. The tetragonal bipyramidal crystals diffract to 3 Angstrom resolution and belong to space group I4(1)22, with unit-cell parameters a = b = 57, c = 207 Angstrom. It is noted that proteins exposed to proteases sometimes yield products that crystallize better than the native molecule and that the beta-subunit of LH represents yet another example. Some indicators of when proteolysis may be a factor in crystallization, as well as some consequences, are described.

引用

页码：872 / 877

页数：6

共 24 条

[1]

Baenziger J.U., 1994, GLYCOPROTEIN HORMONE, P167

[2] The Protein Data Bank [J].