1l4x
From Proteopedia
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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] with MG, CL, NH2 and SIN as ligands. 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 Nov 25 02:30:11 2007
Categories: Protein complex | Aebi, U. | Burkhard, P. | Lustig, A. | Meier, M. | CL | MG | NH2 | SIN | Coiled coil | Ionic interactions | Protein de novo design | Protein folding | Protein oligomerization
