Dynamical properties of fasciculin‐2
Dynamical properties of fasciculin‐2
复制标题
束蛋白-2 的动力学特性
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
J. McCammon
中科院分区：
文献类型：
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作者：
Nathan A. Baker;V. Helms;J. McCammon
Fasciculin-2（FAS 2）是水解酶乙酰胆碱酯酶的有效蛋白质抑制剂。对该毒素进行了2 ns等压等温系综分子动力学模拟，以检查可能在这种抑制中发挥作用的动态结构特性。FAS 2蛋白的构象波动进行了检查，通过各种技术，以确定灵活的残基，并确定其特征运动。毒素“手指”环的尖端和连接环I和II的转弯被发现波动，而蛋白质的其余部分在整个模拟过程中保持相当刚性。最后，将结构波动与相关三指毒素中类似时间尺度上波动的NMR数据进行比较。分子动力学结果与实验测量结果定性一致。蛋白质1999;36：447-453.© 1999 Wiley‐利斯公司
Fasciculin‐2 (FAS2) is a potent protein inhibitor of the hydrolytic enzyme acetylcholinesterase. A 2‐ns isobaric‐isothermal ensemble molecular dynamics simulation of this toxin was performed to examine the dynamic structural properties which may play a role in this inhibition. Conformational fluctuations of the FAS2 protein were examined by a variety of techniques to identify flexible residues and determine their characteristic motion. The tips of the toxin “finger” loops and the turn connecting loops I and II were found to fluctuate, while the rest of the protein remained fairly rigid throughout the simulation. Finally, the structural fluctuations were compared to NMR data of fluctuations on a similar timescale in a related three‐finger toxin. The molecular dynamics results were in good qualitative agreement with the experimental measurements. Proteins 1999;36:447–453. © 1999 Wiley‐Liss, Inc.
影响因子：
4.6
作者：
Jönsson, H;Holm, C;Laurell, T
通讯作者：
Laurell, T