Structural Evolution and Dynamics of the p53 Proteins

被引：41
|
作者：
Chillemi, Giovanni [1 ]
Kehrloesser, Sebastian [2 ]
Bernassola, Francesca [3 ]
Desideri, Alessandro [4 ]
Doetsch, Volker [2 ]
Levine, Arnold J. [5 ,6 ]
Melino, Gerry [7 ]
机构：
[1] CINECA, SCAI SuperComp Applicat & Innovat Dept, I-00185 Rome, Italy
[2] Goethe Univ, Inst Biophys Chem, D-60438 Frankfurt, Germany
[3] Univ Roma Tor Vergata, Dept Expt Med & Surg, I-00133 Rome, Italy
[4] Univ Roma Tor Vergata, Biol Dept, I-00133 Rome, Italy
[5] Inst Adv Study, Olden Lane, Princeton, NJ 08540 USA
[6] Rutgers Canc Inst New Jersey, New Brunswick, NJ 08903 USA
[7] Univ Leicester, Toxicol Unit, Med Res Council, Leicester LE1 9HN, Leics, England
来源：
COLD SPRING HARBOR PERSPECTIVES IN MEDICINE | 2017年 / 7卷 / 04期
基金：
英国医学研究理事会;
关键词：
TUMOR-SUPPRESSOR P53; DNA-BINDING DOMAIN; C-TERMINAL DOMAIN; TETRAMERIZATION DOMAIN; MOLECULAR-DYNAMICS; CRYSTAL-STRUCTURE; MUTANT P53; MATERNAL REPRODUCTION; ENZYME SPECIFICITY; FUNCTIONAL DOMAIN;
D O I：
10.1101/cshperspect.a028308
中图分类号：
R-3 [医学研究方法]; R3 [基础医学];
学科分类号：
1001 ;
摘要：
The family of the p53 tumor suppressive transcription factors includes p73 and p63 in addition to p53 itself. Given the high degree of amino-acid-sequence homology and structural organization shared by the p53 family members, they display some common features (i.e., induction of cell death, cell-cycle arrest, senescence, and metabolic regulation in response to cellular stress) as well as several distinct properties. Here, we describe the structural evolution of the family members with recent advances on the molecular dynamic studies of p53 itself. A crucial role of the carboxy-terminal domain in regulating the properties of the DNA-binding domain (DBD) supports an induced-fit mechanism, in which the binding of p53 on individual promoters is preferentially regulated by the K-OFF over K-ON.
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收藏
页数：15
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