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 language | English (US) |
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Pages (from-to) | 615-617 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 65 |
Issue number | 6 |
DOIs | |
State | Published - 2009 |
Externally published | Yes |
Keywords
- Cell adhesion molecules
- Nectin-2
- V domain
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics