Probing cell-surface architecture through synthesis: an NMR-determined structural motif for tumor-associated mucins.
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.
Live
D H
DH
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Medical School, Minneapolis, MN 55455, USA.
Williams
L J
LJ
Kuduk
S D
SD
Schwarz
J B
JB
Glunz
P W
PW
Chen
X T
XT
Sames
D
D
Kumar
R A
RA
Danishefsky
S J
SJ
D015703:Antigens, CD; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000737:chemistry; D006801:Humans; D051917:Leukosialin; D008969:Molecular Sequence Data; D009077:Mucins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009844:Oligosaccharides / Q000737:chemistry; D012795:Sialoglycoproteins / Q000737:chemistry*
D015703:Antigens, CD; D006020:Glycopeptides; D051917:Leukosialin; D009077:Mucins; D009844:Oligosaccharides; C465014:SPN protein, human; D012795:Sialoglycoproteins