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The fibrillar collagens, collagen VIII, collagen X and the C1q complement proteins share a similar domain in their C‐terminal non‐collagenous regions
Author(s) -
A Brass,
K E Kadler,
J T Thomas,
M E Grant,
R P Boot-Handford
Publication year - 1992
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(92)80503-9
Subject(s) - chemistry , sequence (biology) , c terminus , biochemistry , amino acid , peptide sequence , stereochemistry , biophysics , biology , gene
A sequence comparison of the C‐termini of collagens X, VIII, the collagen‐like complement factor C1q, and the fibrillar collagens showed a conserved cluster of aromatic residues. This conserved cluster was in a domain of approximately 130 amino acids that exhibited marked similarities in hydrophilicity profiles between the different collagens, despite a low level of sequence similarity. These data suggest that the ‘collagen X‐like family’ and the fibrillar collagens contain a domain within their C‐termini that adopts a common tertiary structure, and that a conserved cluster of aromatic residues in this domain may be involved in C‐terminal trimerization.