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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):369-71. doi: 10.1107/S1744309105007475. Epub 2005 Mar 12.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Crystallization / methods
  • Humans
  • Membrane Proteins / chemistry*
  • Occludin
  • Phosphoproteins
  • Protein Structure, Tertiary
  • X-Ray Diffraction
  • Zonula Occludens-1 Protein

Substances

  • Membrane Proteins
  • OCLN protein, human
  • Occludin
  • Phosphoproteins
  • TJP1 protein, human
  • Zonula Occludens-1 Protein