Abstract
Occludin is a tight-junction protein controlling the integrity of endothelial and epithelial cell layers. It forms complexes with the cytoplasmic proteins ZO-1, ZO-2 and ZO-3. The ZO-binding domain in the C-terminal cytoplasmic region of human occludin has previously been isolated and identified. This domain, as expressed in a bacterial system or isolated from native cellular occludin, maintains its ability to bind ZO-1 and ZO-2. The crystallization conditions of the human ZO-binding domain are reported here. The crystals diffract to 2.3 Å resolution and were shown to belong to the orthorhombic space group P212121, with unit-cell parameters a = 33.3, b = 35.4, c = 107.3 Å.
Original language | English (US) |
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Pages (from-to) | 369-371 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 61 |
Issue number | 4 |
DOIs | |
State | Published - 2005 |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics