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
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Medical School, Minneapolis, MN 55455, USA.
Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3489-93. doi: 10.1073/pnas.96.7.3489.
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.
细胞表面粘蛋白糖蛋白会随着肿瘤发生的开始而发生改变。粘蛋白结构的知识可用于针对肿瘤相关粘蛋白基序的疫苗策略。然而，到目前为止，粘蛋白一直难以进行详细的分子分析。本文报道了粘蛋白CD43高度复杂片段的溶液构象。分离出的粘蛋白链的细长二级结构接近折叠蛋白中发现的基序的稳定性。还描述了粘蛋白基序出现所需的特征。相关构建体的免疫特征强烈表明，观察到的表位代表肿瘤细胞表面结构的独特特征。
