Open AccessPurification, crystallization and preliminary X‐ray analysis of the IgV domain of human nectin‐4
Author(s) -
Xu Xiang,
Zhang Xiaoai,
Lu Guangwen,
Cai Yongping
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112027236
Subject(s) - nectin , measles virus , immunoglobulin superfamily , antibody , virus , biology , cell adhesion molecule , microbiology and biotechnology , chemistry , crystallography , cell , virology , cell adhesion , biochemistry , measles , immunology , vaccination
Nectin‐4 belongs to a family of immunoglobulin‐like cell adhesion molecules and is highly expressed in cancer cells. Recently, nectin‐4 was found to be a receptor of measles virus and the IgV domain sustains strong binding to measles virus H protein. In this study, the successful expression and purification of human nectin‐4 V domain (nectin‐4v) is reported. The purified protein was crystallized using the sitting‐drop vapour‐diffusion method. The crystals diffracted to 1.8 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 33.1, b = 51.7, c = 56.9 Å, β = 94.7°. Preliminary analysis of the diffraction data was also performed.