Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|65|6|615-617
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.65, Iss.6, 2009-06, pp. : 615-617
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Abstract
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 P21, with unit‐cell parameters a = 52.3, b = 43.9, c = 56.1 Å, β = 118.2°.
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