Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs
Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs
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DOI：
10.1093/protein/11.6.415
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发表时间：
1998-06-01
期刊：
影响因子：
--
通讯作者：
Silman, I
中科院分区：
文献类型：
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作者：
Botti, SA;Felder, CE;Silman, I
生物大分子表面的静电模体是三维空间中静电势的一种确定的形貌模式，这一概念为识别结构相关大分子表面的功能重要区域提供了强有力的工具。利用这种方法，我们识别了胆碱酯酶(Ches)和一组神经细胞黏附蛋白的共同功能区域，这些蛋白质由于序列高度相似而被认为在结构上与胆碱酯酶有关，但缺乏关键的催化活性丝氨酸，定量分析了乙酰胆碱酯酶活性部位入口周围区域的静电表面电位，与在相似区域内的黏附蛋白的类ChE结构域显示出很好的相关性。这些发现，在先前证据的背景下，涉及到CHS可能的细胞识别功能的相同区域，引导我们定义了一类我们命名为Etactins的黏附蛋白。
The concept of an electrostatic motif on the surface of biological macromolecules as a definite topographical pattern of electrostatic potentials in three-dimensional space, provides a powerful tool for identification of functionally important regions on the surface of structurally related macromolecules, Using this approach, we identify a functional region common to cholinesterases (ChEs) and to a set of neural cell-adhesion proteins that have been suggested to be structurally related to cholinesterases due to their high sequence similarity, but lacking the key catalytically active serine, Quantitative analysis of the electrostatic surface potential in the area surrounding the entrance to the active site of acetylcholinesterase, and in the analogous zone for the ChE-like domain of the adhesion proteins reveals very good correlation. These findings, examined in the context of previous evidence involving this same region in a possible cell-recognition function for ChEs, leads us to define a class of adhesion proteins which we have named 'electrotactins'.