NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.
 

NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

Angew Chem Int Ed Engl. 2020 Aug 03;:

Authors: Jonker HRA, Saxena K, Shcherbakova A, Tiemann B, Bakker H, Schwalbe H

Abstract
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 selective 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.


PMID: 32745319 [PubMed - as supplied by publisher]



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