A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein
✍ Scribed by Beck, Konrad; Gambee, Jay E.; Kamawal, Aqilla; Bächinger, Hans Peter
- Book ID
- 111744853
- Publisher
- Nature Publishing Group
- Year
- 1997
- Tongue
- English
- Weight
- 543 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0261-4189
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The three-dimensional structure of the assembly domain of the cartilage oligomeric matrix protein (COMP) has been modeled. The model demonstrates a parallel five-stranded coiled coil and fits well with a large amount of experimental data that describe the oligomerization state, the a-helical conform
Cartilage oligomeric matrix protein (COMP) is a pentameric glycoprotein of the thrombospondin family found in cartilage and tendon. Self-association of COMP is achieved through the formation of a fivestranded a-helical bundle that involves 64 N-terminal residues (from 20 to 83). The complex is furth