1COS
CRYSTAL STRUCTURE OF A SYNTHETIC TRIPLE-STRANDED ALPHA-HELICAL BUNDLE
Summary for 1COS
| Entry DOI | 10.2210/pdb1cos/pdb |
| Descriptor | COILED SERINE (2 entities in total) |
| Functional Keywords | alpha-helical bundle |
| Total number of polymer chains | 3 |
| Total formula weight | 10007.59 |
| Authors | Lovejoy, B.,Choe, S.,Cascio, D.,Mcrorie, D.K.,Degrado, W.,Eisenberg, D. (deposition date: 1993-01-22, release date: 1993-10-31, Last modification date: 2024-11-06) |
| Primary citation | Lovejoy, B.,Choe, S.,Cascio, D.,McRorie, D.K.,DeGrado, W.F.,Eisenberg, D. Crystal structure of a synthetic triple-stranded alpha-helical bundle. Science, 259:1288-1293, 1993 Cited by PubMed Abstract: The x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple-stranded coiled coil formed by three alpha-helices. Unlike the designed parallel coiled coil, the helices run up-up-down. The structure is stabilized by a distinctive hydrophobic interface consisting of eight layers. As in the design, each alpha-helix in the coiled coil contributes one leucine side chain to each layer. The structure suggests that hydrophobic interactions are a dominant factor in the stabilization of coiled coils. The stoichiometry and geometry of coiled coils are primarily determined by side chain packing in the solvent-inaccessible interior, but electrostatic interactions also contribute. PubMed: 8446897PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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