Molecular dynamics simulations of the O-glycosylated 21-residue MUC1 peptides

A. Rubinstein, L. Kinarsky, S. Sherman

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The conformational propensities of the 21-residue peptide and its O-glycosylated analogs were studied by molecular dynamics (MD) simulations. This polypeptide motif comprises the tandem repeat of the human mucin (MUC1) protein core that is differently glycosylated in normal and cancer cells. To evaluate the structural effects of O-glycosylation on the polypeptide backbone, conformations of the nonglycosylated peptide and its glycosylated analogs were monitored during the 1 ns MD simulations. Radius gyration for whole peptide and its fragments, as well as root-mean-square-deviation between coordinate sets of the backbone atoms of starting structures and generated structures, were calculated. It was shown that O-glycosylation promotes and stabilizes the extended conformations of the whole peptide and its central PDTRP fragment. O-glycosylation of the specific Thr residues significantly affects the conformational distributions of the flanking Ser residues. It was also shown that O-glycosylation promoted backbone conformations of the immunodominant region PDTRP that were similar to the structural features of the peptides presented by the major histocompatability complex (MHC) to T-cell receptors.

Original languageEnglish (US)
Pages (from-to)119-128
Number of pages10
JournalInternational journal of molecular sciences
Volume5
Issue number3
DOIs
StatePublished - Mar 2004

Keywords

  • Conformations
  • Glycopeptide
  • Glycoprotein MUC1
  • Molecular dynamics

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Fingerprint

Dive into the research topics of 'Molecular dynamics simulations of the O-glycosylated 21-residue MUC1 peptides'. Together they form a unique fingerprint.

Cite this