Structural characterization of a mannose-binding protein-trimannoside complex using residual dipolar couplings.
Structural characterization of a mannose-binding protein-trimannoside complex using residual dipolar couplings.
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使用残余偶极耦合对甘露糖结合蛋白-三甘露糖苷复合物进行结构表征。
DOI：
10.1016/s0022-2836(03)00268-7
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发表时间：
2003
影响因子：
5.6
通讯作者：
Prestegard,JamesH
中科院分区：
文献类型：
--
作者：
Jain,NitinU;Noble,Schroeder;Prestegard,JamesH
利用偶极偶联（RDC）研究了来自甘露糖结合蛋白（MBP）的53 kDa同源多聚体三聚体的配体结合特性，RDC可以很容易地从配体和同位素标记蛋白的NMR谱中测量。使用一组有限的1H-15 N骨架酰胺NMR分配MBP和取向信息来自定向介质中的RDC测量，MBP的顺序张量已被确定，这与轴向对称系统的基于能量的预测一致。6-二-O-（α-d-吡喃甘露糖基）-α-d-吡喃甘露糖苷（三甘露糖苷）已在天然丰度下测定并用作取向限制。结合的配体的几何形状和取向的限制允许对接的三甘露糖苷配体的结合位点的MBP产生的MBP-寡糖相互作用的结构模型。
The ligand-binding properties of a 53kDa homomultimeric trimer from mannose-binding protein (MBP) have been investigated using residual dipolar couplings (RDCs) that are easily measured from NMR spectra of the ligand and isotopically labeled protein. Using a limited set of1H–15N backbone amide NMR assignments for MBP and orientational information derived from the RDC measurements in aligned media, an order tensor for MBP has been determined that is consistent with symmetry-based predictions of an axially symmetric system.13C–1H couplings for a bound trisaccharide ligand, methyl 3,6-di-O-(α-d-mannopyranosyl)-α-d-mannopyranoside (trimannoside) have been determined at natural abundance and used as orientational constraints. The bound ligand geometry and orientational constraints allowed docking of the trimannoside ligand in the binding site of MBP to produce a structural model for MBP–oligosaccharide interactions.