Crystal structure of the ENT domain of human EMSY

Chavali, Gayatri B, Ekblad, Caroline M S, Basu, Balaka P, Brissett, Nigel C, Veprintsev, Dmitry, Hughes-Davies, Luke, Kouzarides, Tony, Itzhaki, Laura S and Doherty, Aidan J (2005) Crystal structure of the ENT domain of human EMSY. Journal of Molecular Biology, 350 (5). pp. 964-973. ISSN 0022-2836

Full text not available from this repository.


EMSY is a recently discovered gene encoding a BRCA2-associated protein and is amplified in some sporadic breast and ovarian cancers. The EMSY sequence contains no known domain except for a conserved 100 residue segment at the N terminus. This so-called ENT domain is unique in the human genome, although multiple copies are found in Arabidopsis proteins containing members of the Royal family of chromatin remodelling domains. Here, we report the crystal structure of the ENT domain of EMSY, consisting of a unique arrangement of five a-helices that fold into a helical bundle arrangement. The fold shares regions of structural homology with the DNA-binding domain of homeodomain proteins. The ENT domain forms a homodimer via the anti-parallel packing of the extended N-terminal a-helix of each molecule. It is stabilized mainly by hydrophobic residues at the dimer interface and has a dissociation constant in the low micromolar range. The dimerisation of EMSY mediated by the ENT domain could provide flexibility for it to bind two or more different substrates simultaneously.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Depositing User: Nigel Brissett
Date Deposited: 06 Feb 2012 18:13
Last Modified: 30 Nov 2012 16:59
📧 Request an update