This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1cos
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The x-ray crystal structure of a peptide designed to form a | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 18: | Line 18: | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Lovejoy, B.]] | [[Category: Lovejoy, B.]] | ||
| - | [[Category: Mcrorie, D | + | [[Category: Mcrorie, D K.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: alpha-helical bundle]] | [[Category: alpha-helical bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:11 2008'' |
Revision as of 10:08, 21 February 2008
|
CRYSTAL STRUCTURE OF A SYNTHETIC TRIPLE-STRANDED ALPHA-HELICAL BUNDLE
Overview
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.
About this Structure
1COS is a Protein complex structure of sequences from [1] with and as ligands. The following page contains interesting information on the relation of 1COS with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:08:11 2008
