Qian Xiaomin, Qi Jianxun, Chu Fuliang, Liu Jun, Li Qing, Yan Jinghua
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):615-7. doi: 10.1107/S1744309109016571. Epub 2009 May 22.
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 A resolution and belonged to space group P2(1), with unit-cell parameters a = 52.3, b = 43.9, c = 56.1 A, beta = 118.2 degrees .
NECTIN-2属于免疫球蛋白样细胞粘附分子家族,其特征是细胞外区域存在三个免疫球蛋白样结构域(V、C2和C2)。V结构域在细胞粘附、自然杀伤细胞激活以及某些疱疹病毒的进入中起重要作用。在本研究中,人NECTIN-2的V结构域以包涵体形式在大肠杆菌中表达,随后进行变性和复性。采用悬滴气相扩散法对可溶性蛋白进行结晶。晶体衍射分辨率达到1.85 Å,属于空间群P2(1),晶胞参数为a = 52.3、b = 43.9、c = 56.1 Å,β = 118.2° 。