Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab′ fragment

被引：11

作者：

Spangfort, MD

Mirza, O

Svensson, LA

Larsen, JN

Gajhede, M

Ipsen, H

机构：

[1] ALK Abello, Biochem Allergy Res, DK-2970 Horsholm, Denmark

[2] Univ Copenhagen, Dept Chem, Prot Struct Grp, DK-2100 Copenhagen, Denmark

[3] Univ Lund, Ctr Chem & Chem Engn, Dept Mol Biophys, S-22100 Lund, Sweden

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444999011804

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 A, alpha = 105.7, beta = 98.32, gamma = 97.62 degrees, and diffract to 2.9 Angstrom resolution when analyzed at 100 K using synchrotron-generated X-rays.

引用

页码：2035 / 2036

页数：2

共 11 条

[1] X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy [J].