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J Biomol Struct Dyn. 2006 Aug;24(1):75-82.

Structural differences between wild-type and fish eye disease mutant of lecithin:cholesterol acyltransferase.

Author information

1
Department of Physics, University of Rhode Island, Kingston, Rhode Island 02881, USA. reshetnyak@mail.uri.edu

Abstract

Fluorescence spectroscopy has been used to investigate the conformational changes that occur upon binding of wild type (WT) and mutant (Thr123Ile) lecithin:cholesterol acyltransferase (LCAT) to the potential substrates (dioleoyl-phosphatidyl choline [DOPC] and high density lipoprotein [HDL]). For a detailed analysis of structural differences between WT and mutant LCAT, we performed decompositional analysis of a set of tryptophan fluorescence spectra, measured at increasing concentrations of external quenchers (acrylamide and KI). The data obtained show that Thr123Ile mutation in LCAT leads to a conformation that is likely to be more rigid (less mobile/flexible) than that of the WT protein with a redistribution of charged residues around exposed tryptophan fluorophores. We propose that the redistribution of charged residues in mutant LCAT may be a major factor responsible for the dramatically reduced activity of the enzyme with HDL and reconstituted high density lipoprotein (rHDL).

PMID:
16780378
DOI:
10.1080/07391102.2006.10507101
[Indexed for MEDLINE]

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