NMR Spectroscopic Characterization of the C‐Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach

Autor:	Hendrik R. A. Jonker, Birgit Tiemann, Hans Bakker, Aleksandra Shcherbakova, Krishna Saxena, Harald Schwalbe
Rok vydání:	2020
Předmět:	Glycan Stereochemistry Mannose 010402 general chemistry 01 natural sciences Catalysis chemistry.chemical_compound NMR spectroscopy C-mannosylation ddc:570 conformation analysis Research Articles glycoproteins chemistry.chemical_classification Thrombospondin biology 010405 organic chemistry NMR Spectroscopy | Hot Paper Tryptophan General Chemistry Nuclear magnetic resonance spectroscopy General Medicine 0104 chemical sciences chemistry ddc:540 biology.protein selective isotopic labeling Protein folding Information reporting Glycoprotein Research Article
Zdroj:	Angewandte Chemie (International Ed. in English)
ISSN:	1521-3757 0044-8249
DOI:	10.1002/ange.202009489
Popis:	Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR‐active nuclei. We report on the incorporation of 13C‐labeled mannose in the C‐mannosylated UNC‐5 thrombospondin repeat. The conformational landscape of the C‐mannose sugar puckers attached to tryptophan residues of UNC‐5 is characterized by interconversion between the canonical 1C4 state and the B03 / 1S3 state. This flexibility may be essential for protein folding and stabilization. We foresee that this versatile tool to produce proteins with selectively labeled C‐mannose can be applied and adjusted to other systems and modifications and potentially paves a way to advance glycoprotein research by unravelling the dynamical and conformational properties of glycan structures and their interactions. NMR spectroscopy was used to characterize the C‐mannose conformation in a thrombospondin repeat using a selective labeling approach. The conformational landscape of the C‐mannose sugar puckers attached to tryptophan residues of the netrin receptor UNC‐5 allows interconversion between the canonical 1C4 state and the B03 / 1S3 state.
Databáze:	OpenAIRE
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