Smoothing molecular interactions: The "kinetic buffer" effect of intrinsically disordered proteins
文献类型：期刊论文
| 作者 | Huang, Yongqi1,2,3; Liu, Zhirong1,2,3 |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2010-12-01 |
| 卷号 | 78期号:16页码:3251-3259 |
| 关键词 | Kinetic Buffer Effect Intrinsically Disordered Protein Coupled Folding-binding Fly-casting Mechanism Stabilized Helix |
| ISSN号 | 0887-3585 |
| DOI | 10.1002/prot.22820 |
| 英文摘要 | Intrinsically disordered proteins (IDPs) widely participate in molecular recognition and signaling processes in cells by interacting with other molecules. Compared with ordered proteins, IDPs usually possess stronger intermolecular interactions in binding. As a result, the interface structure of IDPs in complexes is distinct from that of ordered-protein complexes, and this difference may have essential effect on the response to various perturbations in a cell. In this study, we examined the perturbations of intermolecular interactions and temperature on the coupled folding and binding processes of pKID to KIX domains by performing molecular dynamics simulations. By comparing a series of virtual pKID systems with various degree of disorder, we found that the complex stability and the binding kinetics of the disordered systems were less sensitive to the perturbations than the ordered systems. The origin of the lower response sensitivity of IDPs was attributed to their higher flexibility in the complex interface, which was further supported by an analysis on protein complex structures. On the basis of our simulations and results from the literature, we speculate IDPs may not only interact with their biological partners with high specificity and low affinity but also may be resistant to the perturbations in the environment and transmit signals fast and smooth. We proposed to name it the "kinetic buffer" effect. |
| 语种 | 英语 |
| WOS记录号 | WOS:000284046400001 |
| 出版者 | WILEY-BLACKWELL |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/69401]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Liu, Zhirong |
| 作者单位 | 1.Peking Univ, Coll Chem & Mol Engn, State Key Lab Struct Chem Unstable & Stable Speci, Beijing 100871, Peoples R China 2.Peking Univ, Ctr Theoret Biol, Beijing 100871, Peoples R China 3.Peking Univ, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China |
| 推荐引用方式 GB/T 7714 | Huang, Yongqi,Liu, Zhirong. Smoothing molecular interactions: The "kinetic buffer" effect of intrinsically disordered proteins[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2010,78(16):3251-3259. |
| APA | Huang, Yongqi,&Liu, Zhirong.(2010).Smoothing molecular interactions: The "kinetic buffer" effect of intrinsically disordered proteins.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,78(16),3251-3259. |
| MLA | Huang, Yongqi,et al."Smoothing molecular interactions: The "kinetic buffer" effect of intrinsically disordered proteins".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 78.16(2010):3251-3259. |
入库方式： OAI收割
来源：化学研究所
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