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

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.

SUBMITTER: Peng BH

PROVIDER: S-EPMC1952431 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature

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

Peng Bi Hung BH White Mark A MA Campbell Gerald A GA Robert Jebamony J JJ Lee J Ching JC Sutton Roger B RB

Acta crystallographica. Section F, Structural biology and crystallization communications 20050312 Pt 4

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 ...[more]

PMID: 16511043

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