Crystallization and preliminary structural analysis of an antibody complex formed with PfMSP1-19, a malaria vaccine candidate

被引：8

作者：

Pizarro, JC ^{[1
]}

Chitarra, V ^{[1
]}

Calvet, C ^{[1
]}

Verger, D ^{[1
]}

Bentley, GA ^{[1
]}

机构：

[1] Inst Pasteur, CNRS, URA 2185, Unite Immunol Struct, F-75724 Paris, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷

关键词：

D O I：

10.1107/S0907444902007667

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The 11 kDa C-terminal fragment of the proteolyticly matured surface antigen, PfMSP1, from Plasmodium falciparum is a promising malaria vaccine candidate. The soluble recombinant form of this naturally occurring fragment has been crystallized as a complex with the Fab of a specific murine monoclonal antibody. The crystals belong to the space group P2(1), with unit-cell parameters a = 51.8, b = 213.5, c = 60.0 Angstrom, beta =101.0degrees, and with Z = 4. Diffraction data have been measured to 2.9 Angstrom resolution and a preliminary model of the complex has been determined by molecular replacement. The epitope recognised by G17.12 is located on the N-terminal EGF-like domain of the antigen.

引用

页码：1246 / 1248

页数：3

共 11 条

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