Publication Abstract from PubMed
The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three-stranded, alpha-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone alpha-helix and superhelix parameters are consistent with a regular coiled coil structure.
NMR structure of a parallel homotrimeric coiled coil.,Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT Nat Struct Biol. 1998 Aug;5(8):687-91. PMID:9699631[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
