Incorporation of the dopamine D2L receptor and bacteriorhodopsin within bicontinuous cubic lipid phases. 2. Relevance to in meso crystallization of integral membrane proteins in novel lipid systems

被引:34
作者
Conn, Charlotte E. [1 ]
Darmanin, Connie [2 ]
Sagnella, Sharon M. [3 ]
Mulet, Xavier [1 ]
Greaves, Tamar L. [1 ]
Varghese, Joseph N. [2 ]
Drummond, Calum J. [1 ,4 ]
机构
[1] CSIRO Mol & Hlth Technol CMHT, Clayton, Vic 3169, Australia
[2] CSIRO Mol & Hlth Technol CMHT, Parkville, Vic 3052, Australia
[3] CSIRO Mol & Hlth Technol CMHT, N Ryde, NSW 1670, Australia
[4] CSIRO Mat Sci & Engn CMSE, Clayton, Vic 3169, Australia
基金
澳大利亚研究理事会; 美国国家科学基金会;
关键词
SELF-ASSEMBLY MATERIALS; X-RAY-SCATTERING; CRYSTAL-STRUCTURE; MONOOLEIN/WATER SYSTEM; COUPLED RECEPTOR; AGONIST; SCHIZOPHRENIA; INFLAMMATION; SYMPTOMS; BEHAVIOR;
D O I
10.1039/c0sm00464b
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The dopamine D2 long (D2L) receptor and bacteriorhodopsin (bR), which are integral membrane proteins, have been incorporated within bicontinuous cubic mesophases formed by the lipids anandamide and H-farnesoyl monoethanolamide, which have been specifically investigated by us for use as in meso crystallization media. We show that the incorporated membrane protein affects the structure of the cubic phases with the particular effect observed dependent on the geometry of the underlying cubic phase. The results are complementary to those obtained in Part 1 of this series, where we demonstrated that the structural effects observed depend on the structure of the membrane protein. Importantly protein concentrations commonly used for crystallization can destroy the cubic phase matrix, particularly where there is a large discrepancy between the hydrophilic and the hydrophobic spans of the membrane protein, and the hydrophilic and hydrophobic domain sizes of the cubic phase.
引用
收藏
页码:4838 / 4846
页数:9
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