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3GA1

Crystal Structure of the Human Nac1 POZ Domain

Summary for 3GA1
Entry DOI10.2210/pdb3ga1/pdb
DescriptorNucleus accumbens-associated protein 1, NITRATE ION (3 entities in total)
Functional Keywordsbtb/poz domain, nucleus, phosphoprotein, repressor, transcription, transcription regulation
Biological sourceHomo sapiens (Human)
Cellular locationNucleus: Q96RE7
Total number of polymer chains2
Total formula weight28788.50
Authors
Stead, M.A.,Carr, S.B.,Wright, S.C. (deposition date: 2009-02-16, release date: 2009-05-19, Last modification date: 2023-11-01)
Primary citationStead, M.A.,Carr, S.B.,Wright, S.C.
Structure of the human Nac1 POZ domain
Acta Crystallogr.,Sect.F, 65:445-449, 2009
Cited by
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.
PubMed: 19407373
DOI: 10.1107/S1744309109012214
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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