A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix protein

Beck, Konrad ORCID: https://orcid.org/0000-0001-5098-9484, Gambee, J. E., Kamawal, A. and Bächinger, H. P. 1997. A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix protein. EMBO Journal 16 (13) , pp. 3767-3777. 10.1093/emboj/16.13.3767

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Abstract

We have studied the oligomerization of an alpha-helical coiled-coil using as an example a peptide corresponding to the C-terminal domain of cartilage matrix protein. By replacing one arginine residue, which forms an interchain ionic interaction with a glutamic acid residue, with glutamine, we found that this peptide assembles into a homotetramer at neutral pH in contrast to the native molecule which forms homotrimers. At acidic and basic pH, however, we again observed the trimer conformation. Another arginine, which is probably involved in an intrachain salt bridge, has no effect on the assembly. Our data demonstrate that besides the specific distribution of hydrophobic residues, interchain ionic interactions can be crucial in modulating the association behavior of alpha-helical coiled-coil domains.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Subjects:	Q Science > QD Chemistry
Uncontrolled Keywords:	analytical ultracentrifugation, circular dichroism spectroscopy, heptad repeats, ionic interactions, synthetic peptides
Publisher:	NPG
ISSN:	0261-4189
Last Modified:	05 Jan 2024 08:12
URI:	https://orca.cardiff.ac.uk/id/eprint/16307

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