Probing cell-surface architecture through synthesis: An NMR-determined structural motif for tumor-associated mucins

Citation
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
ISSN journal
00278424 → ACNP
Volume
96
Issue
7
Year of publication
1999
Pages
3489 - 3493
Database
ISI
SICI code
0027-8424(19990330)96:7<3489:PCATSA>2.0.ZU;2-G
Abstract
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.