RRC ID 69389
Author Nonaka Y, Ogawa T, Shoji H, Nishi N, Kamitori S, Nakamura T.
Title Crystal structure and conformational stability of a galectin-1 tandem-repeat mutant with a short linker.
Journal Glycobiology
Abstract Modification of the domain architecture of galectins has been attempted to analyze their biological functions and to develop medical applications. Several types of galectin-1 repeat mutants were previously reported but, however, it was not clear whether the native structure of the wild type was retained. In this study, we determined the crystal structure of a galectin-1 tandem-repeat mutant with a short linker peptide, and compared the unfolding profiles of the wild type and mutant by chemical denaturation. The structure of the mutant was consistent with that of the dimer of the wild type, and both carbohydrate-binding sites were retained. The unfolding curve of the wild type with lactose suggested that the dimer dissociation and the tertiary structure unfolding was concomitant at micromolar protein concentrations. The midpoint denaturant concentration of the wild type was dependent on the protein concentration and lower than that of the mutant. Linking the two subunits significantly stabilized the tertiary structure. The mutant exhibited higher T-cell growth-inhibition activity and comparable hemagglutinating activity. Structural stabilization may prevent the oxidation of the internal cysteine residue.
Volume 32(3)
Pages 251-259
Published 2022-3-30
DOI 10.1093/glycob/cwab101
PII 6411845
PMID 34735570
MeSH Binding Sites Carbohydrates / chemistry Galectin 1* / metabolism Galectins* / metabolism Molecular Conformation
IF 4.06
Resource
Human and Animal Cells Jurkat(RCB0806)