Plant Transcription factor database - Universität Potsdam
version: 3.0

Sorghum bicolor SWI/SNF-BAF60b Family

Description

Kussie et al. 1996:The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.

Members of this family
  SHOULD possess SWIB domain

Domain alignments

This family is also present in:

References

There are 13 gene models in this family



Gene modelDescriptionDomains
123164 fgenesh1_pm.C_chr_1000218 DEK_C SWIB
4113286 gw1.8.13005.1 SWIB
4783160 e_gw1.1.5174.1 Plus-3 SWIB
4976562 fgenesh1_pg.C_chr_3003677 Plus-3 SWIB
4996629 estExt_fgenesh1_pg.C_chr_10750 SWIB
4999057 estExt_fgenesh1_pg.C_chr_15129 AT_hook GYF Plus-3 SWIB
5007133 estExt_fgenesh1_pg.C_chr_62523 DEK_C SWIB
5009677 estExt_fgenesh1_pg.C_chr_91440 GYF Plus-3 SWIB
5034745 Sb02g041010 SWIB
5041788 Sb06g016360 SWIB
5053693 Sb03g034370 GYF Plus-3 SWIB
5054613 Sb04g002500 SWIB
5059121 Sb07g028070 SWIB

General references

Bennett-Lovsey, R; Hart, SE; Shirai, H; Mizuguchi, K. 2002. The SWIB and the MDM2 domains are homologous and share a common fold. Bioinformatics 18(4):626-30 PUBMEDID:12016060
Kussie, PH; Gorina, S; Marechal, V; Elenbaas, B; Moreau, J; Levine, AJ; Pavletich, NP. 1996. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274(5289):948-53 PUBMEDID:8875929