Probing cell-surface architecture through synthesis: an NMR-determined structural motif for tumor-associated mucins.
Probing cell-surface architecture through synthesis: an NMR-determined structural motif for tumor-associated mucins.
复制标题
通过合成探测细胞表面结构：核磁共振确定的肿瘤相关粘蛋白的结构基序。
DOI：
10.1073/pnas.96.7.3489
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发表时间：
1999
影响因子：
11.1
通讯作者：
Danishefsky,SJ
中科院分区：
文献类型：
--
作者：
Live,DH;Williams,LJ;Kuduk,SD;Schwarz,JB;Glunz,PW;Chen,XT;Sames,D;Kumar,RA;Danishefsky,SJ
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.
