1D7M
COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I
Summary for 1D7M
| Entry DOI | 10.2210/pdb1d7m/pdb |
| Related | 2ZTA |
| Descriptor | CORTEXILLIN I (2 entities in total) |
| Functional Keywords | coiled-coil, coiled-coil trigger site, alpha helix, dimerization, contractile protein |
| Biological source | Dictyostelium discoideum |
| Total number of polymer chains | 2 |
| Total formula weight | 23246.56 |
| Authors | Burkhard, P.,Kammerer, R.A.,Steinmetz, M.O.,Bourenkov, G.P.,Aebi, U. (deposition date: 1999-10-19, release date: 2000-03-27, Last modification date: 2024-02-07) |
| Primary citation | Burkhard, P.,Kammerer, R.A.,Steinmetz, M.O.,Bourenkov, G.P.,Aebi, U. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure Fold.Des., 8:223-230, 2000 Cited by PubMed Abstract: The parallel two-stranded alpha-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins. The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design. PubMed: 10745004DOI: 10.1016/S0969-2126(00)00100-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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