6FGN

Solution Structure of p300Taz2-p63TA

Summary for 6FGN

• Entry DOI: 10.2210/pdb6fgn/pdb
• NMR Information: BMRB: 34231
• Descriptor: Histone acetyltransferase p300,Tumor protein 63, ZINC ION (2 entities in total)
• Functional Keywords: p300, creb binding protein, p53 family, p63, p73, antitumor protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 14030.25

Authors

Gebel, J.,Kazemi, S.,Lohr, F.,Guntert, P.,Dotsch, V. (deposition date: 2018-01-11, release date: 2018-05-30, Last modification date: 2024-06-19)

Primary citation

Krauskopf, K.,Gebel, J.,Kazemi, S.,Tuppi, M.,Lohr, F.,Schafer, B.,Koch, J.,Guntert, P.,Dotsch, V.,Kehrloesser, S.
Regulation of the Activity in the p53 Family Depends on the Organization of the Transactivation Domain.
Structure, 26:1091-1100.e4, 2018

PubMed Abstract: Despite high sequence homology among the p53 family members, the regulation of their transactivation potential is based on strikingly different mechanisms. Previous studies revealed that the activity of TAp63α is regulated via an autoinhibitory mechanism that keeps inactive TAp63α in a dimeric conformation. While all p73 isoforms are constitutive tetramers, their basal activity is much lower compared with tetrameric TAp63. We show that the dimeric state of TAp63α not only reduces DNA binding affinity, but also suppresses interaction with the acetyltransferase p300. Exchange of the transactivation domains is sufficient to transfer the regulatory characteristics between p63 and p73. Structure determination of the transactivation domains of p63 and p73 in complex with the p300 Taz2 domain further revealed that, in contrast to p53 and p73, p63 has a single transactivation domain. Sequences essential for stabilizing the closed dimer of TAp63α have evolved into a second transactivation domain in p73 and p53.

PubMed: 30099987
DOI: 10.1016/j.str.2018.05.013

Experimental method

SOLUTION NMR