Computational analysis of molecular basis of 1 : 1 interactions of NRG-1 beta wild-type and variants with ErbB3 and ErbB4
文献类型：期刊论文
| 作者 | Luo, C ; Xu, LF; Zheng, SX; Luo, Z; Jiang, XM; Shen, JH; Jiang, HL; Liu, XF; Zhou, MD
|
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2005-06-01 |
| 卷号 | 59期号:4页码:742-756 |
| 关键词 | EGFR NRG-1 beta ErbB ligand-protein interactions binding free energy molecular dynamics MM-PBSA |
| ISSN号 | 0887-3585 |
| DOI | 10.1002/prot.20443 |
| 文献子类 | Article |
| 英文摘要 | The neuregulin/ErbB system is a growth factor/receptor cascade that has been proven to be essential in the development of the heart and the sympathetic nervous system. However, the basis of the specificity of ligand-receptor recognition remains to be elucidated. In this study, the structures of NRG-1 beta/ErbB3 and NRG-1 beta/ErbB4 complexes were modeled based on the available structures of the homologous proteins. The binding free energies of NRG-1 beta to ErbB3 and ErbB4 were calculated using the molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) computational method. In addition, computational alanine-scanning mutagenesis was performed in the binding site of NRG-1 beta and the difference in the binding free energies between NRG-1 beta mutants and the receptors was calculated. The results specify the contribution of each residue at the interaction interfaces to the binding affinity of NRG-1 beta with ErbB3 and ErbB4, identifying several important interaction residue pairs that are in agreement with previously acquired experimental data. This indicates that the presented structural models of NRG-1 beta/ErbB3 and NRG-1 beta/ErbB4 complexes are reliable and could be used to guide future studies, such as performing desirable mutations on NRG-1 beta to increase the binding affinity and selectivity to the receptor and discovering new therapeutic agents for the treatment of heart failure. (c) 2005 Wiley-Liss, Inc. |
| WOS关键词 | EPIDERMAL-GROWTH-FACTOR ; FREE-ENERGY CALCULATIONS ; HEREGULIN BINDING-SITE ; CARDIAC DEVELOPMENT ; EXTRACELLULAR DOMAINS ; NEUREGULIN RECEPTOR ; CONTINUUM SOLVENT ; PROTEIN-PROTEIN ; NERVOUS-SYSTEM ; DYNAMICS |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000229226500008 |
| 出版者 | WILEY-LISS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273869]  |
| 专题 | 新药研究国家重点实验室 中科院受体结构与功能重点实验室 |
| 通讯作者 | Zhou, MD |
| 作者单位 | 1.Zensun Shanghai Sci & Technol Ltd, Shanghai, Peoples R China 2.Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Ctr Drug Discovery & Design, Shanghai 201203, Peoples R China 3.Chinese Acad Sci, Grad Sch, Shanghai, Peoples R China 4.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China |
| 推荐引用方式 GB/T 7714 | Luo, C,Xu, LF,Zheng, SX,et al. Computational analysis of molecular basis of 1 : 1 interactions of NRG-1 beta wild-type and variants with ErbB3 and ErbB4[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2005,59(4):742-756. |
| APA | Luo, C.,Xu, LF.,Zheng, SX.,Luo, Z.,Jiang, XM.,...&Zhou, MD.(2005).Computational analysis of molecular basis of 1 : 1 interactions of NRG-1 beta wild-type and variants with ErbB3 and ErbB4.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,59(4),742-756. |
| MLA | Luo, C,et al."Computational analysis of molecular basis of 1 : 1 interactions of NRG-1 beta wild-type and variants with ErbB3 and ErbB4".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 59.4(2005):742-756. |
入库方式： OAI收割
来源：上海药物研究所
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