Open AccessCrystallization and preliminary X‐ray diffraction of the ZO‐binding domain of human occludin
Author(s) -
Peng BiHung,
White Mark A.,
Campbell Gerald A.,
Robert Jebamony J.,
Lee J. Ching,
Sutton Roger B.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105007475
Subject(s) - occludin , tight junction , cytoplasm , crystallization , microbiology and biotechnology , orthorhombic crystal system , chemistry , crystallography , biophysics , biology , crystal structure , organic chemistry
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 33.3, b = 35.4, c = 107.3 Å.