NMR structure of the principal neutralizing determinant of HIV-1 displayed in filamentous bacteriophage coat protein

Raz Jelinek, Tamsin D. Terry, Jennifer J. Gesell, Pratap Malik, Richard N. Perham, Stanley J. Opella

Research output: Contribution to journalEditorial

49 Scopus citations

Abstract

An NMR approach for structure determination of short peptides displayed on the surface of filamentous bacteriophage virions is demonstrated using the hexapeptide GPGRAF that constitutes the principal neutralizing determinant of HIV-1. This peptide was inserted near the N terminus of the major coat protein of bacteriophage fd. NMR studies of the recombinant protein solubilized in detergent micelles showed that the inserted peptide adopts a double bend S-shaped conformation that is similar to the antibody-bound structure determined by X-ray crystallography. This indicates that a peptide displayed on the bacteriophage coat protein has an enhanced propensity to adopt a conformation similar to that found in the native protein from which it is derived. This approach may be generally applicable to the structure determination of peptide epitopes and other small peptides.

Original languageEnglish
Pages (from-to)649-655
Number of pages7
JournalJournal of Molecular Biology
Volume266
Issue number4
DOIs
StatePublished - 7 Mar 1997
Externally publishedYes

Keywords

  • Epitope
  • NMR
  • Peptide
  • Phage polypeptides
  • Structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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