Abstract: | Comparison of the nucleotide sequence and primary structure of murine and human proα2(I) collage 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-propeptide 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 proα2(I) collagen triple helices, with no truly nonconservative substitutions. |