中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein

文献类型:期刊论文

作者Huang, Yongqi1,2,3; Liu, Zhirong1,2,3
刊名INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
出版日期2011-02-01
卷号12期号:2页码:1410-1430
关键词Anchor Residue Intrinsically Disordered Proteins Binding Promiscuity Molecular Recognition Features P53 Mdm2 Taz2
ISSN号1422-0067
DOI10.3390/ijms12021410
英文摘要Anchor residues, which are deeply buried upon binding, play an important role in protein-protein interactions by providing recognition specificity and facilitating the binding kinetics. Up to now, studies on anchor residues have been focused mainly on ordered proteins. In this study, we investigated anchor residues in intrinsically disordered proteins (IDPs) which are flexible in the free state. We identified the anchor residues of the N-terminus of the p53 protein (Glu17-Asn29, abbreviated as p53N) which are involved in binding with two different targets (MDM2 and Taz2), and analyzed their side chain conformations in the unbound states. The anchor residues in the unbound p53N were found to frequently sample conformations similar to those observed in the bound complexes (i.e., Phe19, Trp23, and Leu26 in the p53N-MDM2 complex, and Leu22 in the p53N-Taz2 complex). We argue that the bound-like conformations of the anchor residues in the unbound state are important for controlling the specific interactions between IDPs and their targets. Further, we propose a mechanism to account for the binding promiscuity of IDPs in terms of anchor residues and molecular recognition features (MoRFs).
语种英语
WOS记录号WOS:000287732000036
出版者MDPI AG
源URL[http://ir.iccas.ac.cn/handle/121111/71725]  
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
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GB/T 7714
Huang, Yongqi,Liu, Zhirong. Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein[J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,2011,12(2):1410-1430.
APA Huang, Yongqi,&Liu, Zhirong.(2011).Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein.INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,12(2),1410-1430.
MLA Huang, Yongqi,et al."Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein".INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 12.2(2011):1410-1430.

入库方式: OAI收割

来源:化学研究所

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