Breaking Pseudo-Symmetry in Multiantennary Complex N-Glycans Using Lanthanide-Binding Tags and NMR Pseudo-Contact Shifts
Breaking Pseudo-Symmetry in Multiantennary Complex N-Glycans Using Lanthanide-Binding Tags and NMR Pseudo-Contact Shifts
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DOI:
10.1002/anie.201307845
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发表时间:
2013-12-16
影响因子:
16.6
通讯作者:
Jimenez-Barbero, Jesus
中科院分区:
文献类型:
--
作者:
Canales, Angeles;Mallagaray, Alvaro;Jimenez-Barbero, Jesus
Molecular recognition is of vital significance for life. Understanding the chemical basis of these interactions between cellular receptors and their specific ligands not only gives a functional meaning to structures and changes occurring in diseases but also helps devise innovative therapeutic approaches. In terms of biological coding and translating signals into cellular effects, glycans have gained a particular status, owing to their unsurpassed coding capacity and widespread presence of receptors (lectins) to read the encoded information.[1] The glycan sequence and shape and the intimate interplay between a glycan determinant and its cognate lectin ensure the flow of information of sugar coding.[2] Thus, in addition to their peptide scaffold, glycoproteins carry a second source of bioinformation in their glycan chains, realized, for example, by recognition of N-glycans by lectins.[3]In this context, we herein present a novel NMR approach to individually monitor the behavior of each arm, A and B, of N-glycans (Scheme 1) and thereby provide a global perspective of their conformational and interaction features in solution. Structurally, N-glycans have a common pentasac-