anchoring intrinsically disordered proteins to multiple targets lessons from n-terminus of the p53 protein锚定内在无序蛋白质多个目标教训p53蛋白的n端.pdfVIP

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anchoring intrinsically disordered proteins to multiple targets lessons from n-terminus of the p53 protein锚定内在无序蛋白质多个目标教训p53蛋白的n端.pdf

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anchoring intrinsically disordered proteins to multiple targets lessons from n-terminus of the p53 protein锚定内在无序蛋白质多个目标教训p53蛋白的n端

Int. J. Mol. Sci. 2011, 12, 1410-1430; doi:10.3390/ijm OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms Article Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein Yongqi Huang 1,2,3 and Zhirong Liu 1,2,3,* 1 State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China 2 Center for Theoretical Biology, Peking University, Beijing 100871, China 3 Beijing National Laboratory for Molecular Sciences, Peking University, Beijing 100871, China * Author to whom correspondence should be addressed; E-Mail: LiuZhiRong@; Tel.: +86-10 Fax: +86-10 Received: 25 January 2011; in revised form: 10 February 2011 / Accepted: 16 February 2011 / Published: 23 February 2011 Abstract: 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