The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin -: Detection of a functional C-type lectin domain with galactose/mannose specificity
The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin -: Detection of a functional C-type lectin domain with galactose/mannose specificity
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DOI：
10.1046/j.1432-1327.2000.01602.x
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发表时间：
2000-08-01
期刊：
影响因子：
--
通讯作者：
Fritz, M
中科院分区：
文献类型：
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作者：
Mann, K;Weiss, IM;Fritz, M
从鲍鱼珍珠层中分离的Perlucin由155个氨基酸组成，包括糖基化的天冬酰胺。前130个氨基酸的序列显示出与去唾液酸糖蛋白受体的C型碳水化合物识别结构域和C型凝集素组的其他成员的高度相似性，但与没有碳水化合物结合活性的相关蛋白质的相似性也较弱。该C型模块之后是短的C末端结构域，其含有两个长度为10个氨基酸的几乎相同的序列重复。固相分析显示perlucin与含有D-半乳糖或D-甘露糖/D-葡萄糖的（新）糖蛋白的二价金属离子依赖性结合，表明perlucin是具有广泛的碳水化合物结合特异性的功能性C型凝集素。我们的研究结果还表明，它可能是难以预测的碳水化合物结合的特异性和发生的替代结合配置的氨基酸序列比较和同源性建模。
Perlucin isolated from abalone nacre consists of 155 amino acids including a glycosylated asparagine. The sequence of the first 130 amino acids shows a high similarity to the C-type carbohydrate-recognition domains of asialoglycoprotein receptors and other members of the group of C-type lectins but also a weaker similarity to related proteins without carbohydrate-binding activity. This C-type module is followed by a short C-terminal domain containing two almost identical sequence repeats with a length of 10 amino acids. Solid phase assays show a divalent metal ion-dependent binding of perlucin to (neo)glycoproteins containing D-galactose or D-mannose/D-glucose indicating that perlucin is a functional C-type lectin with broad carbohydrate-binding specificity. Our results also indicate that it may be difficult to predict carbohydrate-binding specificity and the occurrence of alternative binding configurations by amino-acid sequence comparisons and homology modeling.