Complete primary structure of the α1‐chain of human basement membrane (type IV) collagen

FEBS Letters

Raija, Soininen²  Haka-Risku, Tuula²  Prockop, Darwin J.¹  Tryggvason, Karl² 

[1] Jefferson Institute of Molecular Medicine, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107, USA;Biocenter and Department of Biochemistry, University of Oulu, SF-90570 Oulu, Finland

关键词: Amino acid sequence;    Nucleotide sequence;    Collagen;    Primary structure;    Basement membrane;    (Human);   

DOI  :  10.1016/0014-5793(87)81155-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have determined the primary structure of the α₁(IV)-chain of human type IV collagen by nucleotide sequencing of overlapping cDNA clones that were isolated from a human placental cDNA library. The present data provide the sequence of 295 amino acids not previously determined. Altogether, the α₁(IV)-chain contains 1642 amino acids and has a molecular mass of 157625 Da. There are 1413 residues in the collagenous domain and 229 amino acids in the carboxy-terminal globular domain. The human α₁(IV)-chain contains a total of 21 interruptions in the collagenous Gly-X-Y repeat sequence. These interruptions vary in length between two and eleven residues. The α₁(IV)-chain contains four cysteine residues in the triple-helical domain, four cysteines in the 15-residue long noncollagenous sequence at the amino-terminus and 12 cysteines in the carboxy-terminal NC-domain

【 授权许可】

Unknown