Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule

被引：8

作者：

Abbott, RJM ^{[1
]}

Knott, V ^{[1
]}

Roversi, P ^{[1
]}

Neudeck, S ^{[1
]}

Lukacik, P ^{[1
]}

Handford, PA ^{[1
]}

Lea, SM ^{[1
]}

机构：

[1] Univ Oxford, Dept Biochem, Lab Mol Biophys, Oxford OX1 3QU, England

来源：

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

关键词：

D O I：

10.1107/S0907444904005098

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Crystals of three epidermal growth-factor-like (EGF) domains of EMR2 (143 residues) have been grown. EMR2 is a member of the EGF-TM7 family of proteins. Different splice variants exist with between three and five consecutive EGF modules linked to a seven-span transmembrane G-protein-coupled receptor. Although its precise function is unknown, EMR2 is highly expressed in immune tissues and has been shown to weakly bind CD55, a complement-system regulator. Here, crystallization of EMR2 in the presence of Ca2+, Ba2+ and Sr2+ ions is reported. A complete data set has been collected from all three crystal types, all of which belong to space group P2(1). An anomalous Patterson map from the Ba2+ crystal data reveals three Ba2+ ions bound within the asymmetric unit.

引用

页码：936 / 938

页数：3

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