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PMID: 9233786 Published · ppublish English Journal Article

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

The EMBO journal ·Vol. 16 ·No. 13 ·1997-07-01 ·Pages 3767-77

Beck K, Gambee JE, Kamawal A, Bächinger HP

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.

MeSH Terms
Amino Acid Sequence Animals Arginine/chemistry Cartilage Cartilage Oligomeric Matrix Protein Chickens Extracellular Matrix Proteins Glutamic Acid/chemistry Glutamine/chemistry Glycoproteins/chemistry,metabolism Humans Hydrogen-Ion Concentration Ions Matrilin Proteins Mice Molecular Sequence Data Protein Folding Protein Structure, Secondary
Chemicals
Cartilage Oligomeric Matrix Protein Extracellular Matrix Proteins Glycoproteins Ions Matn1 protein, mouse Matrilin Proteins TSP5 protein, human Glutamine Glutamic Acid Arginine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Beck K
Shriners Hospital for Children, Research Unit, Portland, OR 97201, USA. BECKKO@UMDNJ.EDU
Gambee J E
Kamawal A
Bächinger H P
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/16.13.3767
Email
beckko@umdnj.edu
Published
1997-07-01
Pages
3767-77
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1170000
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/16.13.3767 PMC Full Text View journal details
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