NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the X-ray crystal structures of Pin1
NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the X-ray crystal structures of Pin1
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DOI：
10.1002/bip.10020
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发表时间：
2002-02-01
期刊：
影响因子：
2.9
通讯作者：
Kelly, JW
中科院分区：
文献类型：
--
作者：
Kowalski, JA;Liu, K;Kelly, JW
分离的Apo Pin 1 WW结构域（6-39）的NMR溶液结构显示，它采用扭曲的三链反平行β-折叠构象，非常类似于在双结构域Pin 1蛋白的情况下该结构域的晶体所表现出的结构。虽然载脂蛋白X射线晶体结构中的B因子表明环1和环2在构象上是明确的，但溶液NMR数据表明环1是相当灵活的，至少在不存在配体的情况下是如此。由6-39 Pin 1 WW结构域表现出的NMR化学位移和核Overhauser效应模式已被证明是诊断性的，用于证明该结构域的单位点变体采用正常折叠的结构。在开始进行详细了解β折叠所需的耗时的动力学和热力学研究之前，这种类型的知识至关重要。(C)2002年John Wiley Sons，Inc.
The NMR solution structure of the isolated Apo Pin1 WW domain (6-39) reveals that it adopts a twisted three-stranded antiparallel beta-sheet conformation, very similar to the structure exhibited by the crystal of this domain in the context of the two domain Pin1 protein. While the B factors in the apo x-ray crystal structure indicate that loop 1 and loop 2 are conformationally well defined, the solution NMR data suggest that loop 1 is quite flexible, at least in the absence of the ligand. The NMR chemical shift and nuclear Overhauser effect pattern exhibited by the 6-39 Pin1 WW domain has proven to be diagnostic for demonstrating that single site variants of this domain adopt a normally folded structure. Knowledge of this type is critical before embarking on time-consuming kinetic and thermodynamic studies required for a detailed understanding of beta-sheet folding. (C) 2002 John Wiley Sons, Inc.