Open AccessCrystallization and preliminary X‐ray analysis of the V domain of human nectin‐2
Author(s) -
Qian Xiaomin,
Qi Jianxun,
Chu Fuliang,
Liu Jun,
Li Qing,
Yan Jinghua
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109016571
Subject(s) - immunoglobulin superfamily , nectin , immunoglobulin domain , crystallization , cell adhesion molecule , molecule , cell adhesion , antibody , adhesion , chemistry , crystallography , cell , biophysics , microbiology and biotechnology , biology , biochemistry , immunology , organic chemistry
Nectin‐2 belongs to a family of immunoglobulin‐like cell adhesion molecules that are characterized by the presence of three immunoglobulin‐like domains (V, C2 and C2) in the extracellular region. The V domain plays important roles in cell adhesion, NK cell activation and the entry of some herpesvirus. In this study, the V domain of human nectin‐2 was expressed in Escherichia coli in the form of inclusion bodies, which were subsequently denatured and refolded. The soluble protein was crystallized using the hanging‐drop vapour‐diffusion method. The crystals diffracted to 1.85 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 52.3, b = 43.9, c = 56.1 Å, β = 118.2°.