Acharya K R, Stuart D I, Phillips D C, McKenzie H A, Teahan C G
Department of Biochemistry, University of Bath, England.
J Protein Chem. 1994 Aug;13(6):569-84. doi: 10.1007/BF01901539.
Similarities in amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes have indicated that c-type lysozymes and alpha-lactalbumins are homologous proteins, i.e., descended by divergent evolution from a common ancestor. Like the alpha-lactalbumins, echidna milk, horse milk, and pigeon eggwhite lysozymes all bind Ca(II). Models of their three-dimensional structures, based on their amino acid sequences and the known crystal structures of domestic hen eggwhite and human lysozymes and baboon and human alpha-lactalbumins, have been built. The several structures have been compared and their relationships discussed.
氨基酸序列、三维结构及其基因的外显子 - 内含子模式的相似性表明,c型溶菌酶和α - 乳白蛋白是同源蛋白,即通过趋异进化从共同祖先进化而来。与α - 乳白蛋白一样,针鼹奶、马奶和鸽蛋清溶菌酶都能结合Ca(II)。基于它们的氨基酸序列以及家鸡蛋清、人溶菌酶、狒狒和人α - 乳白蛋白的已知晶体结构,构建了它们的三维结构模型。对这几种结构进行了比较并讨论了它们之间的关系。