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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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📜 SIMILAR VOLUMES


Modeling of a five-stranded coiled coil
✍ Kajava, Andrey V. 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 873 KB

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

Crystallization and preliminary crystall
✍ Efimov, Vladimir P.; Engel, Jürgen; Malashkevich, Vladimir N. 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 374 KB 👁 2 views

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