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

被引:57
作者
Live, DH
Williams, LJ
Kuduk, SD
Schwarz, JB
Glunz, PW
Chen, XT
Sames, D
Kumar, RA
Danishefsky, SJ
机构
[1] Sloan Kettering Inst Canc Res, Bioorgan Chem Lab, New York, NY 10021 USA
[2] Univ Minnesota, Sch Med, Dept Biochem Mol biol & Biophys, Minneapolis, MN 55455 USA
[3] Columbia Univ, Dept Chem, New York, NY 10027 USA
[4] IBM Corp, Thomas J Watson Res Ctr, Computat Biol Ctr, Yorktown Hts, NY 10598 USA
关键词
D O I
10.1073/pnas.96.7.3489
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:3489 / 3493
页数:5
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