α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily
| Autor: | David J.S. Hulmes, Audrey McAlinden, Damien Ficheux, David A.D. Parry, Linda J. Sandell, Thomasin A. Smith |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Repetitive Sequences Amino Acid Fibrillar Collagens Recombinant Fusion Proteins viruses Sequence alignment Biology Biochemistry Protein Structure Secondary Protein structure Collagen VI von Willebrand Factor Humans Protein oligomerization Amino Acid Sequence Molecular Biology Peptide sequence Coiled coil Cell Biology Peptide Fragments Protein Structure Tertiary Heptad repeat Biophysics Collagen Sequence Alignment Procollagen Triple helix |
| Zdroj: | Journal of Biological Chemistry. 278:42200-42207 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m302429200 |
| Popis: | Alpha-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. |
| Databáze: | OpenAIRE |
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