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Structure of the human Nac1 POZ domain

DOI: 10.1107/S1744309109012214 DOI Help
PMID: 19407373 PMID Help

Authors: Mark Stead (Institute of Molecular and Cellular Biology, University of Leeds) , Stephen Carr (Membrane Protein Laboratory, Diamond Light Source) , Stephanie Wright (Institute of Molecular and Cellular Biology, University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 65 , PAGES 445 - 449

State: Published (Approved)
Published: May 2009
Diamond Proposal Number(s): 302

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 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 [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.

Journal Keywords: Conserved; Crystallography; X-Ray; Humans; Models; Molecular; Neoplasm; Protein; Tertiary; Repressor; Sequence Alignment

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I03-Macromolecular Crystallography

Added On: 17/08/2011 13:01

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