Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation
文献类型：期刊论文
| 作者 | Yue, LD; Ye, F; Gui, CS; Luo, HB; Cai, JH; Shen, JH ; Chen, KX; Shen, X; Jiang, HL
|
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2005-03 |
| 卷号 | 14期号:3页码:812-822 |
| 关键词 | liver X receptor (LXR) peroxisome proliferator-activated receptor (PPAR) retinoid X receptor (RXR) surface plasmon resonance (SPR) kinetic analysis molecular dynamics (MD) simulation |
| ISSN号 | 0961-8368 |
| DOI | 10.1110/ps.04951405 |
| 文献子类 | Article |
| 英文摘要 | Liver X receptor (LXR) and peroxisome proliferator-activated receptor (PPAR) are two members of nuclear receptors involved in the nutrient metabolisms of dietary fatty acid and cholesterol. They are found to be of cross-talk function in that LXR regulates fatty acid synthesis and PPAR controls fatty acid degradation. LXRs (LXRalpha and LXRbeta) function by forming obligate heterodimers with the retinoid X receptor (RXR), and subsequently binding to specific DNA response elements within the regulatory regions of their target genes. In this work, the kinetic features concerning LXR/RXR and LXR/PPAR interactions have been fully investigated using surface plasmon resonance (SPR) technology. It is found that LXRs could bind to all the three PPAR subtypes, PPARalpha, PPARgamma and PPARdelta with different binding affinities, and such receptor/receptor interactions could be regulated by ligand binding. Moreover, molecular dynamics (MD) simulations were performed on six typical complex models. The results revealed that ligands may increase the interaction energies between the receptor interfaces of the simulated receptor/receptor complexes. The MD results are in agreement with the SPR data. Further analyses on the MD results indicated that the ligand binding might increase the hydrogen bonds between the interfaces of the receptor/receptor complex. |
| WOS关键词 | PROLIFERATOR-ACTIVATED RECEPTOR ; SURFACE-PLASMON RESONANCE ; FATTY-ACID-METABOLISM ; RETINOID-X-RECEPTOR ; NUCLEAR RECEPTOR ; CRYSTAL-STRUCTURE ; PPAR-GAMMA ; CROSS-TALK ; NUTRITIONAL REGULATION ; PROTEIN INTERACTIONS |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000227116400026 |
| 出版者 | COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273905]  |
| 专题 | 药理学第三研究室 中科院受体结构与功能重点实验室 新药研究国家重点实验室 药物发现与设计中心 |
| 通讯作者 | Shen, X |
| 作者单位 | 1.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci,Shanghai Inst Mat Med, State Key Lab Drug Res,Drug Discovery & Design Ct, Shanghai 201203, Peoples R China 2.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yue, LD,Ye, F,Gui, CS,et al. Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation[J]. PROTEIN SCIENCE,2005,14(3):812-822. |
| APA | Yue, LD.,Ye, F.,Gui, CS.,Luo, HB.,Cai, JH.,...&Jiang, HL.(2005).Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation.PROTEIN SCIENCE,14(3),812-822. |
| MLA | Yue, LD,et al."Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation".PROTEIN SCIENCE 14.3(2005):812-822. |
入库方式： OAI收割
来源：上海药物研究所
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