Structure and function in the p53 family

被引:98
作者
Arrowsmith, CH
机构
[1] Univ Toronto, Ontario Canc Inst, Toronto, ON M5G 2M9, Canada
[2] Univ Toronto, Dept Med Biophys, Toronto, ON M5G 2M9, Canada
基金
英国医学研究理事会;
关键词
tumor suppressor; SAM domain; oligomerization; protein-protein interaction;
D O I
10.1038/sj.cdd.4400619
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The recent discovery of several p53 homologs has uncovered a p53 superfamily of transcription factors that can trigger cell cycle arrest and apoptosis. The challenge now is to understand the similarities and differences between family members especially in terms of their regulation and potential for physical or genetic interactions with one another. This review summarizes recent progress in understanding the structure-function relationship within the p53 family. The new family members, p63 and p73, have an additional conserved domain at their C-termini which may have a regulatory function. The structure of this domain (a SAM domain) suggests that it is a protein-protein interaction module that may be involved in developmental processes. The oligomerization domains of p53 family members, while conserved in sequence and three dimensional structure do not interact appreciably with other family members, but do mediate interactions between the multiple splice variants from an individual gene.
引用
收藏
页码:1169 / 1173
页数:5
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