Premium
The gene for the alpha 1(IV) chain of human type IV procollagen: the exon structures do not coincide with the two structural subdomains in the globular carboxy‐terminus of the protein.
Author(s) -
Soininen R.,
Chow L.,
Kurkinen M.,
Tryggvason K.,
Prockop D.J.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04574.x
Subject(s) - biology , exon , procollagen peptidase , alpha (finance) , gene , peptide sequence , genetics , microbiology and biotechnology , globular protein , biochemistry , medicine , construct validity , nursing , patient satisfaction
Previous studies on the coding sequences of DNAs for the alpha 1(IV) chain of basement membrane collagen demonstrated a striking homology between the first 115 and the second 114 amino acids of the globular (NC1) domain of the protein. Also, alignment of the 12 cysteine residues indicated that the homology was particularly strong around three paired clusters of amino acids around cysteine residues. Here we have isolated a cosmid clone containing the 3′‐end of the gene. Analysis of the clone and previously isolated lambda clones demonstrated that the intron‐‐exon patterns of the gene does not reflect the homology in the protein. Therefore the homology cannot have arisen in any simple manner from gene duplications.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom