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Crystallization and preliminary X-ray analysis of the V domain of human nectin-2.

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 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 .

SUBMITTER: Qian X

PROVIDER: S-EPMC2688424 | biostudies-other | 2009 Jun

REPOSITORIES: biostudies-other

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Crystallization and preliminary X-ray analysis of the V domain of human nectin-2.

Qian Xiaomin X Qi Jianxun J Chu Fuliang F Liu Jun J Li Qing Q Yan Jinghua J

Acta crystallographica. Section F, Structural biology and crystallization communications 20090522 Pt 6

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 ...[more]

PMID: 19478445

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