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Structural studies of the neural-cell-adhesion molecule by X-ray and neutron reflectivity.

机译:通过X射线和中子反射率研究神经细胞粘附分子的结构。

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The structures of adhesion proteins play an important role in the formation of intercellular junctions and the control of intermembrane spacing. This paper describes the combination of neutron and X-ray specular reflectivity measurements to investigate the structure of the ectodomain of the neural-cell-adhesion molecule (NCAM). The measurements with unmodified NCAM suggest the presence of a bend in the extracellular region. Measurements with the polysialic-acid-modified form of NCAM reveal that, at physiological ionic strength, the carbohydrate chains extend beyond the range of the unmodified protein. The excluded volume of the polymer is also ionic-strength-dependent, as expected for a polyelectrolyte. The structural characteristics obtained from these independent analyses of X-ray and neutron reflectivity data agree with each other, with prior reflectivity studies, and with molecular dimensions obtained from direct-force measurements. These results provide structural insights into the configuration of the NCAM ectodomain and the regulation of NCAM adhesion by post-translational modification.
机译:粘附蛋白的结构在细胞间连接的形成和膜间间距的控制中起重要作用。本文介绍了中子和X射线镜面反射率测量的组合,以研究神经细胞粘附分子(NCAM)胞外域的结构。使用未修饰的NCAM进行的测量表明细胞外区域存在弯曲。用NCAM的多唾液酸修饰形式进行的测量表明,在生理离子强度下,碳水化合物链延伸超出了未修饰蛋白质的范围。如聚电解质所预期的,聚合物的排除体积也取决于离子强度。通过对X射线和中子反射率数据的这些独立分析获得的结构特征与先前的反射率研究以及通过直接力测量获得的分子尺寸相互一致。这些结果提供了对NCAM胞外域的配置和NCAM粘附通过翻译后修饰的调节的结构见解。

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