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PDBsum entry 2nn2
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Transcription
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PDB id
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2nn2
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the btb domain from the lrf/zbtb7 transcriptional regulator.
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Authors
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P.J.Stogios,
L.Chen,
G.G.Privé.
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Ref.
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Protein Sci, 2007,
16,
336-342.
[DOI no: ]
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PubMed id
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Abstract
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BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in
development, differentiation, and oncogenesis. In these proteins, the BTB domain
(also known as the POZ domain) is a protein-protein interaction motif that
contains a dimerization interface, a possible oligomerization surface, and
surfaces for interactions with other factors, including nuclear co-repressors
and histone deacetylases. The BTB-ZF protein LRF (also known as ZBTB7, FBI-1,
OCZF, and Pokemon) is a master regulator of oncogenesis, and represses the
transcription of a variety of important genes, including the ARF, c-fos, and
c-myc oncogenes and extracellular matrix genes. We determined the crystal
structure of the BTB domain from human LRF to 2.1 A and observed the canonical
BTB homodimer fold. However, novel features are apparent on the surface of the
homodimer, including differences in the lateral groove and charged pocket
regions. The residues that line the lateral groove have little similarity with
the equivalent residues from the BCL6 BTB domain, and we show that the
17-residue BCL6 Binding Domain (BBD) from the SMRT co-repressor does not bind to
the LRF BTB domain.
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