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

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|61|4|369-371

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.61, Iss.4, 2005-04, pp. : 369-371

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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.