2KZS

DAXX helical bundle (DHB) domain

Summary for 2KZS

• Entry DOI: 10.2210/pdb2kzs/pdb
• NMR Information: BMRB: 17018
• Descriptor: Death-associated protein 6 (1 entity in total)
• Functional Keywords: helical bundle, dhb domain, fas death-domain associated protein, daxx, rassf1c interacting domain, apoptosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 10950.83

Authors

Escobar-Cabrera, E.,Lau, D.K.W.,Giovinazzi, S.,Ishov, A.M.,McIntosh, L.P. (deposition date: 2010-06-23, release date: 2010-12-15, Last modification date: 2024-05-15)

Primary citation

Escobar-Cabrera, E.,Lau, D.K.,Giovinazzi, S.,Ishov, A.M.,McIntosh, L.P.
Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C.
Structure, 18:1642-1653, 2010

PubMed Abstract: DAXX is a scaffold protein with diverse roles including transcription and cell cycle regulation. Using NMR spectroscopy, we demonstrate that the C-terminal half of DAXX is intrinsically disordered, whereas a folded domain is present near its N terminus. This domain forms a left-handed four-helix bundle (H1, H2, H4, H5). However, due to a crossover helix (H3), this topology differs from that of the Sin3 PAH domain, which to date has been used as a model for DAXX. The N-terminal residues of the tumor suppressor Rassf1C fold into an amphipathic α helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) ∼60 μM). Based on a proposed DAXX recognition motif as hydrophobic residues preceded by negatively charged groups, we found that peptide models of p53 and Mdm2 also bound the helical bundle. These data provide a structural foundation for understanding the diverse functions of DAXX.

PubMed: 21134643
DOI: 10.1016/j.str.2010.09.016

Experimental method

SOLUTION NMR