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Purification, crystallization and preliminary X-ray analysis of the IgV domain of human nectin-4.

ABSTRACT: Nectin-4 belongs to a family of immunoglobulin-like cell adhesion molecules and is highly expressed in cancer cells. Recently, nectin-4 was found to be a receptor of measles virus and the IgV domain sustains strong binding to measles virus H protein. In this study, the successful expression and purification of human nectin-4 V domain (nectin-4v) is reported. The purified protein was crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to 1.8?Å resolution and belonged to space group P2(1), with unit-cell parameters a = 33.1, b = 51.7, c = 56.9?Å, ? = 94.7°. Preliminary analysis of the diffraction data was also performed.

SUBMITTER: Xu X

PROVIDER: S-EPMC3412779 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of the IgV domain of human nectin-4.

Xu Xiang X Zhang Xiaoai X Lu Guangwen G Cai Yongping Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20120731 Pt 8

Nectin-4 belongs to a family of immunoglobulin-like cell adhesion molecules and is highly expressed in cancer cells. Recently, nectin-4 was found to be a receptor of measles virus and the IgV domain sustains strong binding to measles virus H protein. In this study, the successful expression and purification of human nectin-4 V domain (nectin-4v) is reported. The purified protein was crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to 1.8 Å resolution and belon ...[more]

PMID: 22869128

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