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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment.
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Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment.

机译:结晶和初步的x射线分析桦树花粉过敏原Bet v 1在复杂鼠单克隆免疫球蛋白Fab片段。

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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 A resolution when analyzed at 100 K using synchrotron-generated X--rays.
机译:人类的I型过敏反应特点是存在的有浓度过敏原特异性血清免疫球蛋白E (IgE)。Allergen-mediated receptor-bound的交联表面IgE肥大细胞和循环嗜碱粒细胞触发介质的释放,导致临床的发展过敏的症状。allergen-antibody基础结构之间的互动,一个复杂的专业桦树花粉过敏原Bet v 1和一个工厂的片段从小鼠单克隆Bet v 1孤立抗体BV16结晶。水晶属于空间群P1,晶胞参数= 91.65,= 99.14 b, c = 108.90,α= 105.7,β= 98.32,γ= 97.622.9度,衍射分辨率时分析了在使用synchrotron-generated 100 KX -射线。

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