Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen. Academic Article

abstract

• We have determined the primary structure of the alpha 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 alpha 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 alpha 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 alpha 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.

authors

• Prockop, Darwin

published proceedings

• FEBS Lett

altmetric score

• 6

author list (cited authors)

• Soininen, R., Haka-Risku, T., Prockop, D. J., & Tryggvason, K.

citation count

• 99

complete list of authors

• Soininen, R||Haka-Risku, T||Prockop, DJ||Tryggvason, K

publication date

• December 1987

publisher

• Wiley  Publisher

published in

• FEBS Letters  Journal

keywords

• Amino Acid Sequence
• Base Sequence
• Basement Membrane
• Collagen
• DNA
• DNA, Recombinant
• Disulfides
• Female
• Humans
• Molecular Sequence Data
• Placenta
• Pregnancy
• Repetitive Sequences, Nucleic Acid

PubMed Central ID

• 3691802

Digital Object Identifier (DOI)

• 10.1016/0014-5793(87)81155-9

start page

• 188

end page

• 194

volume

• 225

issue

• 1-2

URL

• http://dx.doi.org/10.1016/0014-5793(87)81155-9