Structural highlights
Function
MATN1_CHICK Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT. NMR structure of a parallel homotrimeric coiled coil. Nat Struct Biol. 1998 Aug;5(8):687-91. PMID:9699631 doi:10.1038/1382
