Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes.

Article Details

Citation

Su MW, Benson-Chanda V, Vissing H, Ramirez F

Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes.

Genomics. 1989 Apr;4(3):438-41.

PubMed ID
2714801 [ View in PubMed
]
Abstract

The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Collagen alpha-1(II) chainP02458Details