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Probing Cell-Surface Architecture through Synthesis: An NMR-Determined Structural Motif for Tumor-Associated Mucins

Live, David H. ; Williams, Lawrence J. ; Kuduk, Scott D. ; Schwarz, Jacob B. ; Glunz, Peter W. ; Chen, Xiao-Tao ; Sames, Dalibor ; Kumar, R. Ajay ; Danishefsky, Samuel J.

Proceedings of the National Academy of Sciences - PNAS, 1999-03, Vol.96 (7), p.3489-3493 [Revista revisada por pares]

United States: National Academy of Sciences of the United States of America

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Probing Cell-Surface Architecture through Synthesis: An NMR-Determined Structural Motif for Tumor-Associated Mucins
Autor: Live, David H. ; Williams, Lawrence J. ; Kuduk, Scott D. ; Schwarz, Jacob B. ; Glunz, Peter W. ; Chen, Xiao-Tao ; Sames, Dalibor ; Kumar, R. Ajay ; Danishefsky, Samuel J.
Materias: Amides ; Antigens ; Antigens, CD ; Biochemistry ; Carbohydrate Conformation ; Carbohydrate Sequence ; Cellular biology ; Glycopeptides - chemistry ; Glycoproteins ; Humans ; Leukosialin ; Molecular Sequence Data ; Mucins ; Mucins - chemistry ; NMR ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Oligosaccharides - chemistry ; Physical Sciences ; Polysaccharides ; Proteins ; Protons ; Scaffolds ; Sialoglycoproteins - chemistry ; Spectroscopy ; Sugars ; Tumors
Es parte de: Proceedings of the National Academy of Sciences - PNAS, 1999-03, Vol.96 (7), p.3489-3493
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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To whom reprint requests should be addressed. e-mail: s-danishefsky@ski.mskcc.org.
Contributed by Samuel J. Danishefsky
Descripción: 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.
Editor: United States: National Academy of Sciences of the United States of America
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Probing Cell-Surface Architecture through Synthesis: An NMR-Determined Structural Motif for Tumor-Associated Mucins

Live, David H. ; Williams, Lawrence J. ; Kuduk, Scott D. ; Schwarz, Jacob B. ; Glunz, Peter W. ; Chen, Xiao-Tao ; Sames, Dalibor ; Kumar, R. Ajay ; Danishefsky, Samuel J.

United States: National Academy of Sciences of the United States of America

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