Crystallization and preliminary X-ray analysis of the V domain of human nectin-2.
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 .
Qian
Xiaomin
X
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Qi
Jianxun
J
Chu
Fuliang
F
Liu
Jun
J
Li
Qing
Q
Yan
Jinghua
J
D000595:Amino Acid Sequence; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D003625:Data Collection; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D000075983:Nectins; D010957:Plasmids; D011489:Protein Denaturation; D020673:Protein Renaturation; D017434:Protein Structure, Tertiary; D012995:Solubility; D013223:Statistics as Topic; D013696:Temperature; D014169:Transformation, Bacterial; D014961:X-Ray Diffraction
D015815:Cell Adhesion Molecules; D000075983:Nectins