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The C-terminal domain of matrilin-2 assembles into a three-stranded alpha-helical coiled coil

Pan, O. H. and Beck, Konrad 1998. The C-terminal domain of matrilin-2 assembles into a three-stranded alpha-helical coiled coil. Journal of Biological Chemistry 273 (23) , pp. 14205-14209. 10.1074/jbc.273.23.14205

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Matrilin-2 is a member of von Willebrand factor A containing extracellular matrix proteins in which the cDNA-derived sequence shows similar domain organization to cartilage matrix protein/matrilin-1, but information on the protein structure is limited. Here we studied the oligomerization potential of a synthetic peptide NH2-ENLILFQNVANEEVRKLTQRLEEMTQRMEALENRLKYR-COOH corresponding to the C-terminal sequence of mouse matrilin-2. The central portion of this sequence shows a periodicity of hydrophobic residues occupying positions a and d of a heptad pattern (abcdefg)n, which is characteristic for alpha-helical coiled-coil proteins. Circular dichroism spectroscopy revealed a high alpha-helical content, and the shape of the spectra is indicative for a coiled-coil conformation. Chemical cross-linking and size exclusion chromatography suggest a homotrimeric configuration. Thermal denaturation in benign buffer shows a single cooperative transition with DeltaH0 = -375 kJ/mol. Melting temperatures Tm varied from 38 to 51 degreesC within a concentration range of 10 to 85 microM, which is about 35 degreesC lower than determined for a peptide corresponding to the C-terminal domain of matrilin-1. The data suggest that despite the low sequence identity within this region, matrilin-2 will form a homotrimer as matrilin-1 does.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > QD Chemistry
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Date of First Compliant Deposit: 7 June 2016
Last Modified: 04 Jun 2017 03:04

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