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

Bihung Peng, Mark White, Gerald Campbell, Jebamony J. Robert, James Lee, Roger B. Sutton

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)369-371
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number4
DOIs
StatePublished - 2005

Fingerprint

Occludin
Crystallization
X-Ray Diffraction
crystallization
X ray diffraction
diffraction
Tight Junction Proteins
proteins
x rays
Endothelial cells
integrity
Endothelial Cells
Epithelial Cells
Crystals
cells
crystals
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin. / Peng, Bihung; White, Mark; Campbell, Gerald; Robert, Jebamony J.; Lee, James; Sutton, Roger B.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 4, 2005, p. 369-371.

Research output: Contribution to journalArticle

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AU - Sutton, Roger B.

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