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Complete primary structure of the α 1 ‐chain of human basement membrane (type IV) collagen
Author(s) -
Raija Soininen,
Haka-Risku Tuula,
Prockop Darwin J.,
Tryggvason Karl
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81155-9
Subject(s) - basement membrane , protein primary structure , type iv collagen , chemistry , primary (astronomy) , chain (unit) , membrane , type (biology) , biophysics , crystallography , biochemistry , geology , microbiology and biotechnology , peptide sequence , biology , laminin , extracellular matrix , physics , gene , paleontology , astronomy
We have determined the primary structure of the α 1 (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 α 1 (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 α 1 (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 α 1 (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