1AQ5
HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE TRIMERIC COILED-COIL DOMAIN OF CHICKEN CARTILAGE MATRIX PROTEIN, 20 STRUCTURES
Summary for 1AQ5
| Entry DOI | 10.2210/pdb1aq5/pdb |
| Descriptor | CARTILAGE MATRIX PROTEIN (1 entity in total) |
| Functional Keywords | coiled-coil, heptad repeat, interchain disulfide bonds, oligomerization domain, trimer, cartilage matrix protein, matrilin-1, noncollagenous extracellular protein |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 3 |
| Total formula weight | 16179.76 |
| Authors | Dames, S.A.,Wiltscheck, R.,Kammerer, R.A.,Engel, J.,Alexandrescu, A.T. (deposition date: 1997-08-07, release date: 1998-02-11, Last modification date: 2024-11-06) |
| Primary citation | Dames, S.A.,Kammerer, R.A.,Wiltscheck, R.,Engel, J.,Alexandrescu, A.T. NMR structure of a parallel homotrimeric coiled coil. Nat.Struct.Biol., 5:687-691, 1998 Cited by PubMed Abstract: 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. PubMed: 9699631DOI: 10.1038/1382 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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