| Primary Identifier | IPR038163 | Type | Homologous_superfamily |
| Short Name | Dro_p53_C_sf |
| description | The p53 tumour suppressor [, , , , ]is a protein found in increased amounts in a wide variety of transformed cells. It is also detectable in many proliferating non-transformed cells, but it is undetectable or present at low levels in resting cells. It is frequently mutated or inactivated in many types of cancer. p53 seems to act as a tumour suppressor in some, but probably not all, tumour types. p53 has been implicated in cell cycle regulation, particularly in the monitoring of genomic DNA integrity prior to replication; for this reason it has been dubbed `guardian of the genome'. p53 is a sequence-specific DNA-binding protein and transcription factor. The structure of p53 comprises 4 domains: an N-terminal transactivation domain; a central DNA-binding domain; an oligomerisation domain; and a C-terminal, basic, regulatory domain [, ]. The structure of the oligomerisation domain consists of a dimer of dimers, each dimer consisting of 2 anti-parallel α-helices and an anti-parallel β-sheet. The sheets lie on opposite sides of the tetramer and the helices form an unusual 4-helix bundle [, ]. While the majority of p53 mutations found in human cancers are located in the DNA-binding domain, some are also found in the oligomerisation domain.This entry represents the C-terminal domain of Drosophila transcription factor p53. While the rest of the protein is quite conserved between the different transcription factors such as p53 and p73, the C-terminal domain is highly divergent. The Drosophila p53 structure is characterised by an additional N-terminal β-strand and a C-terminal helix []. |
