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

Xiaomin Qian, Jianxun Qi, Fuliang Chu, Jun Liu, Qing Li, Jinghua Yan

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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°.

Original languageEnglish (US)
Pages (from-to)615-617
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number6
DOIs
StatePublished - 2009
Externally publishedYes

Keywords

  • Cell adhesion molecules
  • Nectin-2
  • V domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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