Malectin is a membrane-anchored endoplasmic reticulum (ER)-resident lectin, which is first identified in Xenopus laevis in 2008 and highly conserved among animals. Malectin plays an important role in the quality control of glycoprotein in the ER through recognizing the GlcManGlcNAc (G2M9) oligosaccharide chain on the newly synthesized glycoproteins. In this chapter, we will describe the preparation of recombinant soluble malectin and its tetramer, which might be developed as useful tools for detection of Glcα1-3Glc containing glycans on the cell surface.
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http://dx.doi.org/10.1007/978-1-0716-0430-4_28 | DOI Listing |
Methods Mol Biol
March 2021
Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Chiba, Japan.
Int J Mol Sci
May 2017
Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 Chemin de Borde Rouge, Auzeville, BP 42617, 31326 Castanet-Tolosan, France.
Lectins are fundamental to plant life and have important roles in cell-to-cell communication; development and defence strategies. At the cell surface; lectins are present both as soluble proteins (LecPs) and as chimeric proteins: lectins are then the extracellular domains of receptor-like kinases (LecRLKs) and receptor-like proteins (LecRLPs). In this review; we first describe the domain architectures of proteins harbouring G-type; L-type; LysM and malectin carbohydrate-binding domains.
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