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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):369-71. Epub 2005 Mar 12.

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

Author information

1
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555, USA.

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 A resolution and were shown to belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 33.3, b = 35.4, c = 107.3 A.

PMID:
16511043
PMCID:
PMC1952431
DOI:
10.1107/S1744309105007475
[Indexed for MEDLINE]
Free PMC Article

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