Crystallization and preliminary X-ray analysis of the complex between human CTLA-4 and B7-2

X. Zhang, J. C D Schwartz, S. G. Nathenson, Steven C. Almo

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

CTLA-4 is a dimeric T-cell surface receptor responsible for transducing signals that down-regulate activated T cells upon binding B7 ligands. The disulfide-linked homodimer of the extracellular segment of human CTLA-4 and the receptor-binding domain of human B7-2 were purified and cocrystallized. Diffraction from these crystals is consistent with the monoclinic space group P21 (unit-cell parameters a = 47.85, b = 54.56, c = 103.09 Å, β = 91.63); native data have been collected to 3.2 Å resolution.

Original languageEnglish (US)
Pages (from-to)898-899
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number6
DOIs
StatePublished - 2001

Fingerprint

T-cells
X ray analysis
Crystallization
X-Rays
crystallization
Cell Surface Receptors
disulfides
T-Cell Antigen Receptor
Disulfides
x rays
Down-Regulation
Diffraction
Ligands
T-Lymphocytes
Crystals
ligands
cells
diffraction
crystals

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Crystallization and preliminary X-ray analysis of the complex between human CTLA-4 and B7-2. / Zhang, X.; Schwartz, J. C D; Nathenson, S. G.; Almo, Steven C.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 6, 2001, p. 898-899.

Research output: Contribution to journalArticle

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