Dh. Live et al., Probing cell-surface architecture through synthesis: An NMR-determined structural motif for tumor-associated mucins, P NAS US, 96(7), 1999, pp. 3489-3493
Citations number
33
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Cell-surface mucin glycoproteins are altered with the onset of oncogenesis,
Knowledge of mucin structure could be used in vaccine strategies that targ
et tumor-associated mucin motifs, Thus far, however, mucins have resisted d
etailed molecular analysis. Reported herein is the solution conformation of
a highly complex segment of the mucin CD43. The elongated secondary struct
ure of the isolated mucin strand approaches the stability of motifs found i
n folded proteins. The features required for the mucin motif to emerge are
also described. Immunocharacterization of related constructs strongly sugge
sts that the observed epitopes represent distinguishing features of tumor c
ell-surface architecture.