Human basement membrane collagen (type IV). The amino acid sequence of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain reveals deletions in the alpha 1(IV) chain.
The cDNA and protein sequences of the N-terminal 60% of the alpha 2(IV) chain of human basement membrane collagen have been determined. By repeated primer extension with synthetic oligodeoxynucleotides and mRNA from either HT1080 cells or human placenta overlapping clones were obtained which cover 3414 bp. The derived protein sequence allows for the first time a comparison and alignment of both alpha chains of type IV collagen from the N terminus. This alignment reveals an additional 43 amino acid residues in the alpha 2(IV) chain as compared to the alpha 1(IV) chain. 21 of these additional residues form a disulfide-bridged loop within the triple helix which is unique among all known collagens.
Brazel
D
D
Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Pollner
R
R
Oberbäumer
I
I
Kühn
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001483:Base Sequence; D001485:Basement Membrane / Q000032:analysis*; D003001:Cloning, Molecular; D003094:Collagen / Q000032:analysis*; D004247:DNA / Q000032:analysis; D006801:Humans; D008969:Molecular Sequence Data
D000596:Amino Acids; D003094:Collagen; D004247:DNA