title: 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.
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.
authors.affiliation: Department of Microbiology and Immunology, Morse Institute of Molecular Genetics, State University of New York Health Science Center, Brooklyn 11203.
authors.forename: M W
authors.initials: MW
authors.lastname: Su
authors.forename: V
authors.initials: V
authors.lastname: Benson-Chanda
authors.forename: H
authors.initials: H
authors.lastname: Vissing
authors.forename: F
authors.initials: F
authors.lastname: Ramirez
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D002417:Cattle / Q000235:genetics; D003094:Collagen / Q000235:genetics; D005091:Exons; D005796:Genes; D006801:Humans; D008969:Molecular Sequence Data; D011347:Procollagen / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
chemical_list: D011347:Procollagen; D003094:Collagen