A recombinant polypeptide, composed of the α-helical neck region and the carbohydrate recogniton domain of conglutinin, self-associates to give a functionally intact homotrimer

Jiu Yao Wang, Uday Kishore, Kenneth B.M. Reid

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

A recombinant polypeptide composed of the α-helical neck region and carbohydrate recognition domain (CRD) of bovine conglutinin was expressed in Escherichia coli. The recombinant protein formed inclusion bodies but could be solubilised using a denaturation-renaturation cycle based on urea and then purified by affinity chromatography on a TSK-N-acetylglucosamine column. The purified product behaved as a homotrimer in nondissociating conditions, with three CRDs held together by the α-helical neck regions. The trimer, although lacking the N-terminal and collagen regions of the native conglutinin, showed the same binding carbohydrate specificities as the native molecule, for the complement fragment C3b and for lipopolysaccharides derived from Gram-negative bacteria.

Original languageEnglish
Pages (from-to)6-10
Number of pages5
JournalFEBS Letters
Volume376
Issue number1-2
DOIs
Publication statusPublished - 1995 Nov 27

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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