Phillips C L, Morgan A L, Lever L W, Wenstrup R J
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
Genomics. 1992 Aug;13(4):1345-6. doi: 10.1016/0888-7543(92)90065-z.
Comparison of the nucleotide sequence and primary structure of murine and human pro alpha 2(I) collagen indicates a high degree of homology: 87% at the nucleotide level and 87% at the amino acid level, with the greatest degree of variability in the amino- and carboxy-pro-peptide domains. The homology is greatest in the triple helical domain, repeating [Gly-X-Y]338, exhibiting 90% homology at the amino acid level, with only X and Y position residue substitutions. The X and Y residues show 86% homology between murine and human pro alpha 2(I) collagen triple helices, with no truly nonconservative substitutions.
小鼠和人原α2（I）型胶原蛋白的核苷酸序列及一级结构比较显示出高度同源性：核苷酸水平为87%，氨基酸水平为87%，在氨基和羧基前肽结构域的变异性最大。在三螺旋结构域同源性最高，重复[甘氨酸-X-Y]338，在氨基酸水平上表现出90%的同源性，只有X和Y位置的残基发生取代。小鼠和人原α2（I）型胶原蛋白三螺旋结构中的X和Y残基显示出86%的同源性，没有真正的非保守取代。
