Open AccessStructure of the human Nac1 POZ domain
Author(s) -
Stead Mark A.,
Carr Stephen B.,
Wright Stephanie C.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109012214
Subject(s) - zinc finger , transcription factor , transcription (linguistics) , microbiology and biotechnology , biology , domain (mathematical analysis) , dna binding domain , hamp domain , protein domain , chemistry , genetics , gene , mathematics , mathematical analysis , linguistics , philosophy
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 Å 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 α‐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.