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对一种与结合和未结合肽的P-糖蛋白特异性结合的Fab片段进行的初步晶体学分析。

Preliminary crystallographic analysis of a Fab specific for P-glycoprotein with and without bound peptide.

作者信息

Vasudevan S, Johns K L, Rose D R

机构信息

Department of Medical Biophysics, University of Toronto, Ontario Cancer Institute, Canada.

出版信息

J Mol Biol. 1994 Sep 2;241(5):736-8. doi: 10.1006/jmbi.1994.1548.

Abstract

The antigen-binding fragment (Fab) of anti-peptide monoclonal antibody C219 raised against the multidrug resistance associated P-glycoprotein has been crystallized with and without bound peptide. The crystals of the Fab in the absence and presence of peptide belong to space groups P2(1) and P2(1)2(1)2(1), respectively. The volumes of both crystal forms are consistent with the presence of four Fab molecules per asymmetric unit. Diffraction data to 3.2 A resolution have been collected on a San Diego Multiwire Area Detector system from both crystal forms. Determination of the molecular replacement solutions is underway.

摘要

针对多药耐药相关P-糖蛋白产生的抗肽单克隆抗体C219的抗原结合片段(Fab),在有和没有结合肽的情况下都已结晶。不存在肽和存在肽时Fab的晶体分别属于空间群P2(1)和P2(1)2(1)2(1)。两种晶体形式的体积都与每个不对称单元存在四个Fab分子一致。已在圣地亚哥多丝面积探测器系统上收集了两种晶体形式分辨率达3.2埃的衍射数据。分子置换解的确定正在进行中。

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