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首页> 外文期刊>Journal of Molecular Biology >Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes.
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Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes.

机译：p53衍生的配体与MDM2的结合可诱导多种长距离构象变化。

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摘要

We have used NMR to study the effects of peptide binding on the N-terminal p53-binding domain of human MDM2 (residues 25-109). There were changes in HSQC-chemical shifts throughout the domain on binding four different p53-derived peptide ligands that were significantly large to be indicative of global conformational changes. Large changes in chemical shift were observed in two main regions: the peptide-binding cleft that directly binds the p53 ligands; and the hinge regions connecting the beta-sheet and alpha-helical structures that form the binding cleft. These conformational changes reflect the adaptation of the cleft on binding peptide ligands that differ in length and amino acid composition. Different ligands may induce different conformational transitions in MDM2 that could be responsible for its function. The dynamic nature of MDM2 might be important in the design of anti-cancer drugs that are targeted to its p53-binding site.
机译：我们已使用NMR研究了肽结合对人MDM2（残基25-109）的N末端p53结合域的影响。在结合四个不同的p53衍生肽配体时，整个结构域的HSQC化学位移发生了变化，这些变化显着很大，可以指示整体构象变化。在两个主要区域观察到化学位移的大变化：直接结合p53配体的肽结合裂;铰链区连接形成折叠裂缝的β-折叠和α-螺旋结构。这些构象变化反映了裂缝在长度和氨基酸组成不同的结合肽配体上的适应性。不同的配体可能在MDM2中诱导不同的构象转变，这可能与其功能有关。 MDM2的动态性质可能在设计针对其p53结合位点的抗癌药物中很重要。

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