Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin.
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.
Peng
Bi Hung
BH
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555, USA.
White
Mark A
MA
Campbell
Gerald A
GA
Robert
Jebamony J
JJ
Lee
J Ching
JC
Sutton
Roger B
RB
D001665:Binding Sites; D003460:Crystallization / Q000379:methods; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D062793:Occludin; D010750:Phosphoproteins; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction; D062826:Zonula Occludens-1 Protein
D008565:Membrane Proteins; C568985:OCLN protein, human; D062793:Occludin; D010750:Phosphoproteins; C569042:TJP1 protein, human; D062826:Zonula Occludens-1 Protein