Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex

被引:14
作者
Himanen, JP [1 ]
Nikolov, DB [1 ]
机构
[1] Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444902000264
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Eph receptors and their ephrin ligands are involved in various aspects of cell-cell communication during development, including those of the axon pathfinding processes in the nervous system and cell-cell interactions of the vascular endothelial cells. The recognition and binding properties of the ligand-binding domain of EphB2 receptor and the extracellular domain of ephrin-B2 have been studied and two different cocrystals of their complex have been generated. One crystal form has space group C2, diffracts to 3.5 Angstrom and has unit-cell parameters a = 128, b = 88, c = 79 Angstrom, beta = 112degrees. The other crystal form grows in space group P1, has unit-cell parameters a = 78, b = 78, c = 78 Angstrom, alpha = 69, beta = 75, gamma = 69degrees and diffracts to 2.7 Angstrom. Structure-determination experiments using the latter form are in progress. The structure of the complex will elucidate the chemical nature of the interactions between Eph receptors and ephrins, which would create the possibility of using them as targets for structure-based anticancer-drug development.
引用
收藏
页码:533 / 535
页数:3
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