3GA1

Structure of the human Nac1 POZ domain

(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 445-449

• PubMed: 19407373 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309109012214
• Primary Citation of Related Structures:  
  3GA1


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Institute of Molecular and Cellular Biology, University of Leeds, England, UK.