Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of a synthetic triple-stranded alpha-helical bundle.,Lovejoy B, Choe S, Cascio D, McRorie DK, DeGrado WF, Eisenberg D Science. 1993 Feb 26;259(5099):1288-93. PMID:8446897[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lovejoy B, Choe S, Cascio D, McRorie DK, DeGrado WF, Eisenberg D. Crystal structure of a synthetic triple-stranded alpha-helical bundle. Science. 1993 Feb 26;259(5099):1288-93. PMID:8446897
