一种抑制酶活性的抗HIV-1蛋白酶抗体的初步晶体学研究。
Preliminary crystallographic studies of an anti-HIV-1 protease antibody that inhibits enzyme activity.
作者信息
Lescar J, Stouracova R, Riottot M M, Chitarra V, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley G A
机构信息
Unité d'Immunologie Structurale, Institut Pasteur, Paris, France.
出版信息
Protein Sci. 1996 May;5(5):966-8. doi: 10.1002/pro.5560050518.
Abstract
F11.2.32, a monoclonal antibody directed against the HIV-1 protease, displays strong inhibitory effects toward the catalytic activity of the enzyme. The antibody cross-reacts with peptides 36-46 and 36-57 from the protease. Crystals of the Fab have been obtained both in the free state and as complexes formed with the protease peptide fragments, 36-46 and 36-57. Diffraction data have been collected for the free and complexed forms of Fab F11.2.32 and preliminary models for the crystal structures were obtained by molecular replacement.
摘要
F11.2.32是一种针对HIV-1蛋白酶的单克隆抗体，对该酶的催化活性具有强烈的抑制作用。该抗体与蛋白酶的36-46和36-57肽段发生交叉反应。已分别获得游离状态以及与蛋白酶肽段36-46和36-57形成复合物状态的Fab晶体。已收集了Fab F11.2.32游离形式和复合形式的衍射数据，并通过分子置换获得了晶体结构的初步模型。
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