Authors: | Live, D. H.; Williams, L. J.; Kuduk, S. D.; Schwarz, J. B.; Glunz, P. W.; Chen, X. T.; Sames, D.; Kumar, R. A.; Danishefsky, S. J. |
Article Title: | Probing cell-surface architecture through synthesis: An NMR-determined structural motif for tumor-associated mucins |
Abstract: | Cell-surface mucin glycoproteins are altered with the onset of oncogenesis. Knowledge of mucin structure could be used in vaccine strategies that target tumor-associated mucin motifs. Thus far, however, mucins have resisted detailed molecular analysis. Reported herein is the solution conformation of a highly complex segment of the mucin CD43. The elongated secondary structure of the isolated mucin strand approaches the stability of motifs found in folded proteins. The features required for the mucin motif to emerge are also described. Immunocharacterization of related constructs strongly suggests that the observed epitopes represent distinguishing features of tumor cell-surface architecture. |
Keywords: | protein conformation; protein stability; leukosialin; molecular sequence data; tumor cell; antigens, cd; protein folding; protein secondary structure; structure analysis; nuclear magnetic resonance; carbohydrate sequence; glycopeptides; mucin; cell surface; mucins; nuclear magnetic resonance, biomolecular; carbohydrate conformation; oligosaccharides; cytoarchitecture; protein glycosylation; nuclear overhauser effect; humans; priority journal; article; sialoglycoproteins; antigens, cd43 |
Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
Volume: | 96 |
Issue: | 7 |
ISSN: | 0027-8424 |
Publisher: | National Academy of Sciences |
Date Published: | 1999-03-01 |
Start Page: | 3489 |
End Page: | 3493 |
Language: | English |
DOI: | 10.1073/pnas.96.7.3489 |
PUBMED: | 10097062 |
PROVIDER: | scopus |
PMCID: | PMC22319 |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |