'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks.
'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks.
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DOI：
10.1021/ja4056678
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发表时间：
2013-11-13
影响因子：
15
通讯作者：
Davis BG
中科院分区：
文献类型：
--
作者：
Barry CS;Cocinero EJ;Carçabal P;Gamblin DP;Stanca-Kaposta EC;Remmert SM;Fernández-Alonso MC;Rudić S;Simons JP;Davis BG
真核生物蛋白质的N-糖基化是普遍存在的，对生存至关重要。五糖单元-Man 3GlcNAc 2-位于在此过程中连接到天冬酰胺侧链的所有寡糖的蛋白质连接核心。虽然它的绝对保守意味着一个不可或缺的作用，与它的结构，它的无偏构象和潜在的调节作用的溶剂化是未知的，现在都已经通过合成，激光光谱学和计算相结合的探索。近端的− GlcNAc-GlcNAc-单元作为刚性杆，而中心的不寻常的−Man-β-1，4-GlcNAc-连接更灵活，并由远端的Man-α-1，3-和Man-α-1，6-分支单元调节。溶剂化使“棒”变硬，但通过β-Man枢轴使远端残基保持柔性，确保从蛋白质壳锚定突出，同时允许N-糖基化的远端部分与本体水和生物分子组装体的柔性相互作用。
N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit −Man3GlcNAc2– lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal −GlcNAc-GlcNAc– unit acts as a rigid rod, while the central, and unusual, −Man-β-1,4-GlcNAc– linkage is more flexible and is modulated by the distal Man-α-1,3– and Man-α-1,6– branching units. Solvation stiffens the ‘rod’ but leaves the distal residues flexible, through a β-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies.
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影响因子：
5.2
作者：
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通讯作者：
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影响因子：
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影响因子：
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作者：
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