Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop

Kengo Kitadokoro, Marco Ponassi, Giuliano Galli, Roberto Petracca, Fabiana Falugi, Guido Grandi, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

The large extracellular loop of human CD81, a tetraspanin mediating hepatitis C virus envelope protein E2 binding to human cells, has been crystallized in a hexagonal form. The three-dimensional structure, solved and refined at 2.6 Å resolution (R-factor = 22.8%), shows that the protein adopts a dimeric assembly, based on an association interface built up by tetraspanin-conserved residues. Structural comparisons with the tertiary structure of human CD81 large extracellular loop, previously determined in a different crystal form, show marked conformational fluctuations in the molecular regions thought to be involved in binding to the viral protein, suggesting rules for recognition and assembly within the tetraspan web.

Original languageEnglish
Pages (from-to)1447-1452
Number of pages6
JournalBiological Chemistry
Volume383
Issue number9
DOIs
Publication statusPublished - Sep 1 2002

Keywords

  • CD81
  • HCV E2 glycoprotein
  • Hepatitis C virus
  • Receptor protein
  • Tetraspanins

ASJC Scopus subject areas

  • Biochemistry

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