Transient protein-protein interactions visualized by solution NMR
文献类型：期刊论文
| 作者 | Liu, Zhu1,2,3; Gong, Zhou1; Dong, Xu1; Tang, Chun1 |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2016 |
| 卷号 | 1864期号:1页码:115-122 |
| 关键词 | Nuclear magnetic resonance Chemical shift perturbation Paramagnetic relaxation enhancement Protein-protein interaction Ensemble averaging Fleeting interaction |
| 英文摘要 | Proteins interact with each other to establish their identities in cell. The affinities for the interactions span more than ten orders of magnitude, and K-D values in M-mM regimen are considered transient and are important in cell signaling. Solution NMR including diamagnetic and paramagnetic techniques has enabled atomic resolution depictions of transient protein-protein interactions. Diamagnetic NMR allows characterization of protein complexes with K-D values up to several mM, whereas ultraweak and fleeting complexes can be modeled with the use of paramagnetic NMR especially paramagnetic relaxation enhancement (PRE). When tackling ever larger protein complexes, PRE can be particularly useful in providing long-range intermolecular distance restraints. As NMR measurements are averaged over the ensemble of complex structures, structural information for dynamic protein-protein interactions besides the stereospecific one can often be extracted. Herein the protein interaction dynamics are exemplified by encounter complexes, alternative binding modes, and coupled binding/folding of intrinsically disordered proteins. Further integration of NMR with other biophysical techniques should allow better visualization of transient protein-protein interactions. In particular, single molecule data may facilitate the interpretation of ensemble-averaged NMR data. Though same structures of proteins and protein complexes were found in cell as in diluted solution, we anticipate that the dynamics of transient protein protein-protein interactions be different, which awaits awaits exploration by NMR. This article is part of a Special Issue entitled: Physiological Enzymology and Protein Functions. (C) 2015 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | INTRINSICALLY DISORDERED PROTEINS ; RESIDUAL DIPOLAR COUPLINGS ; PARAMAGNETIC RELAXATION ENHANCEMENT ; INTERMOLECULAR DISTANCE RESTRAINTS ; SINGLE-MOLECULE FRET ; ESCHERICHIA-COLI ; PHOSPHOTRANSFERASE SYSTEM ; MULTIDIMENSIONAL NMR ; MANNITOL TRANSPORTER ; ENCOUNTER COMPLEXES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000370464300013 |
| 公开日期 | 2016-04-26 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/9196]  |
| 专题 | 武汉物理与数学研究所_磁共振应用研究部 |
| 作者单位 | 1.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom Mol Phys, Wuhan Inst Phys & Math, CAS Key Lab Magnet Resonance Biol Syst, Wuhan 430071, Hubei Province, Peoples R China 2.Zhejiang Univ, Sch Med, Dept Pharmacol, Hangzhou 310028, Zhejiang, Peoples R China 3.Zhejiang Univ, Sch Med, Inst Neurosci, Hangzhou 310028, Zhejiang, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Zhu,Gong, Zhou,Dong, Xu,et al. Transient protein-protein interactions visualized by solution NMR[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2016,1864(1):115-122. |
| APA | Liu, Zhu,Gong, Zhou,Dong, Xu,&Tang, Chun.(2016).Transient protein-protein interactions visualized by solution NMR.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1864(1),115-122. |
| MLA | Liu, Zhu,et al."Transient protein-protein interactions visualized by solution NMR".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1864.1(2016):115-122. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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