1l4x
From Proteopedia
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1D7M, 1HQJ, 1KYC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
octameric de novo designed peptide
Overview
Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions.
About this Structure
1L4X is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide., Meier M, Lustig A, Aebi U, Burkhard P, J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:12064934
Page seeded by OCA on Sun Mar 30 21:58:03 2008
