3ga1

Publication Abstract from PubMed

Nac1 is a POZ-domain transcription factor that is involved in the self-renewal of embryonic stem cells. It is overexpressed in ovarian serous carcinoma and targeting the interactions of its POZ domain is a potential therapeutic strategy. Nac1 lacks a zinc-finger DNA-binding domain and thereby differs from most other POZ-domain transcription factors. Here, the crystal structure of the Nac1 POZ domain at 2.1 A resolution is reported. The Nac1 POZ domain crystallized as a dimer in which the interaction interfaces between subunits resemble those found in the POZ-zinc finger transcription factors. The organization of the Nac1 POZ-domain core resembles reported POZ-domain structures, whereas the C-terminus differs markedly. The C-terminal alpha-helix of the Nac1 POZ domain is shorter than that observed in most other POZ-domain transcription factors; variation in the organization of this region may be a general feature of POZ-domain structures.

Structure of the human Nac1 POZ domain.,Stead MA, Carr SB, Wright SC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):445-9. Epub 2009 Apr 24. PMID:19407373^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.