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Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein
Huang, Yongqi1,2,3; Liu, Zhirong1,2,3
2011-02-01
Source PublicationINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
ISSN1422-0067
Volume12Issue:2Pages:1410-1430
AbstractAnchor 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).
KeywordAnchor Residue Intrinsically Disordered Proteins Binding Promiscuity Molecular Recognition Features P53 Mdm2 Taz2
DOI10.3390/ijms12021410
Indexed BySCI
Language英语
WOS IDWOS:000287732000036
PublisherMDPI AG
Citation statistics
Cited Times:16[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.iccas.ac.cn/handle/121111/71726
Collection中国科学院化学研究所
Corresponding AuthorLiu, Zhirong
Affiliation1.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
Recommended Citation
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.
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