α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily

• Published in: The Journal of biological chemistry 2003-10, Vol.278 (43), p.42200-42207
• Main Authors: McAlinden, Audrey, Smith, Thomasin A., Sandell, Linda J., Ficheux, Damien, Parry, David A.D., Hulmes, David J.S.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Biochemistry, Molecular Biology; Collagen - chemistry; Fibrillar Collagens - chemistry; Humans; Life Sciences; Models, Molecular; Peptide Fragments - chemistry; Procollagen - chemistry; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Fusion Proteins; Repetitive Sequences, Amino Acid; Sequence Alignment; von Willebrand Factor - chemistry
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M302429200

α-Helical coiled coils are widely occurring protein oligomerization motifs. Here we show that most members of the collagen superfamily contain short, repeating heptad sequences typical of coiled coils. Such sequences are found at the N-terminal ends of the C-propeptide domains in all fibrillar procollagens. When fused C-terminal to a reporter molecule containing a collagen-like sequence that does not spontaneously trimerize, the C-propeptide heptad repeats induced trimerization. C-terminal heptad repeats were also found in the oligomerization domains of the multiplexins (collagens XV and XVIII). N-terminal heptad repeats are known to drive trimerization in transmembrane collagens, whereas fibril-associated collagens with interrupted triple helices, as well as collagens VII, XIII, XXIII, and XXV, were found to contain heptad repeats between collagen domains. Finally, heptad repeats were found in the von Willebrand factor A domains known to be involved in trimerization of collagen VI, as well as in collagen VII. These observations suggest that coiled-coil oligomerization domains are widely used in the assembly of collagens and collagen-like proteins.