Molecular and Structural Basis for Sugar Recognition by Mannose 6-Phosphate Receptor Homology Domain-Containing Lectins and Proteins

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  • Satoh Tadashi
    Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan

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  • マンノース6 リン酸受容体相同ドメインを有するレクチンおよびタンパク質による糖鎖認識の分子構造基盤

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Abstract

N-Linked glycans play important roles in the determination of glycoprotein fates in cells through interactions with a variety of intracellular lectins. Most of the intracellular lectins possess carbohydrate recognition domain, which is homologous to legume lectins or mannose 6-phosphate receptors (MPRs). These lectins are categorized as L-type or P-type lectins. Besides L-type lectins, recently accumulated frontal affinity chromatography and glycan microarray data have demonstrated that P-type lectins and the MPR homology (MRH) domain-containing proteins have distinct sugar-binding specificity profiles. Furthermore, newly emerged three-dimensional structural data have revealed sugar recognition mechanisms at an atomic level. This review summarizes the current state of knowledge of molecular and structural basis for sugar recognition by P-type lectins and MRH domain-containing proteins that control folding, transport, and degradation of N-linked glycoproteins in the secretory pathway.

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