Crystallisation of membrane proteins mediated by antibody fragments

被引：142

作者：

Hunte, C ^{[1
]}

Michel, H ^{[1
]}

机构：

[1] Max Planck Inst Biophys, Abt Mol Membranbiol, D-60528 Frankfurt, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2002年 / 12卷 / 04期

关键词：

D O I：

10.1016/S0959-440X(02)00354-8

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：

X-ray structures of three different membrane proteins in complex with antibody fragments have been published. The binding of Fv or Fab fragments enlarges the hydrophilic part of integral membrane proteins, thereby providing additional surface for crystal contacts and space for the detergent micelle. In all reported cases, antibody binding was either essential for the crystallisation of the membrane protein or it substantially improved the diffraction quality of the crystals. Antibody-fragment-mediated crystallisation appears to be a valuable tool in particular for membrane proteins with very small hydrophilic or flexible domains.

引用

页码：503 / 508

页数：6

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