title: Sequence analysis of a full-length cDNA for the murine pro alpha 2(I) collagen chain: comparison of the derived primary structure with human pro alpha 2(I) collagen.
abstract: 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.
authors.affiliation: Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
authors.forename: C L
authors.initials: CL
authors.lastname: Phillips
authors.forename: A L
authors.initials: AL
authors.lastname: Morgan
authors.forename: L W
authors.initials: LW
authors.lastname: Lever
authors.forename: R J
authors.initials: RJ
authors.lastname: Wenstrup
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011347:Procollagen / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D011347:Procollagen; D004247:DNA