Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 4 (April 2005)

crystallization communications

Acta Cryst. (2005). F61, 369-371 [ doi:10.1107/S1744309105007475 ]

Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin

B.-H. Peng, M. A. White, G. A. Campbell, J. J. Robert, J. C. Lee and R. B. Sutton

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.

Keywords: occludin; tight junction.


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