CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF A MONOCLONAL-ANTIBODY FAB FRAGMENT SPECIFIC FOR AN INFLUENZA-VIRUS HEMAGGLUTININ AND OF AN ESCAPE MUTANT OF THAT HEMAGGLUTININ

被引:8
作者
BIZEBARD, T
MAUGUEN, Y
PETEK, F
RIGOLET, P
SKEHEL, JJ
KNOSSOW, M
机构
[1] CNRS,UPR 180,CTR PHARMACEUT,PHYS LAB,F-92296 CHATENAY MALABRY,FRANCE
[2] INST RECH SCI CANC,BIOL MOLEC INTERFERONS LAB,CNRS,UPR 37,F-94802 VILLEJUIF,FRANCE
[3] NATL INST MED RES,LONDON NW7 1AA,ENGLAND
关键词
D O I
10.1016/0022-2836(90)90378-Y
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
Preliminary crystallographic data are given for two molecules involved in the interaction between the humoral immune response and the influenza virus. These molecules are the Fab fragment of an antibody specific for the haemagglutinin of influenza virus strain X31 (Hong Kong 1/68 (H3N2)) and a mutant of X31 haemagglutinin that escapes recognition by that antibody. Crystals of the haemagglutinin are isomorphous to those of X31, whose structure is known; they diffract to 3.4 Å resolution. Crystals of the Fab fragment are trigonal with space group P3121 (or P3221 and diffract to 2.6 Å resolution. The unit cell dimensions are a = b = 98.9 A ̊, c = 89.2 A ̊. A native data set has been collected for both proteins. © 1990.
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页码:513 / 514
页数:2
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