| First Author | Phillips CL | Year | 1992 |
| Journal | Genomics | Volume | 13 |
| Issue | 4 | Pages | 1345-6 |
| PubMed ID | 1505972 | Mgi Jnum | J:1726 |
| Mgi Id | MGI:50252 | Doi | 10.1016/0888-7543(92)90065-z |
| Citation | Phillips CL, et al. (1992) 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. Genomics 13(4):1345-6 |
| abstractText | 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. |
