NMR structure of a parallel homotrimeric coiled coil.
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.
Department of Structural Biology, Biozentrum, University of Basel, Switzerland.
S A
SA
Dames
R A
RA
Kammerer
R
R
Wiltscheck
J
J
Engel
A T
AT
Alexandrescu
D000595:Amino Acid Sequence; D000818:Animals; D002356:Cartilage / Q000737:chemistry*; D002645:Chickens; D003198:Computer Simulation; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000235:genetics; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics; D064235:Matrilin Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D064235:Matrilin Proteins; D011994:Recombinant Proteins