The fibrillar collagens, collagen VIII, collagen X and the C1q complement proteins share a similar domain in their C-terminal non-collagenous regions.
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.
Brass
A
A
Department of Biochemistry and Molecular Biology, University of Manchester, UK.
Kadler
K E
KE
Thomas
J T
JT
Grant
M E
ME
Boot-Handford
R P
RP
D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry*; D015922:Complement C1q / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D015922:Complement C1q; D003094:Collagen