Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding
Article Abstract:
A structure of the DNA-binding domain (DBD) of human regulatory factor X1 (hRFX1) is presented, binding cooperatively to a symmetrical X-box. hRFX1 is in the winged-helix subfamily of helix-turn-helix proteins, and its uses a beta-hairpin to recognize DNA. A new model for linker histone and DNA interactions is proposed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Crystal structure of TFIID TATA-box binding protein
Article Abstract:
The molecular form of the TATA-box binding protein (TBP or TFIID-tau) has been determined using X-ray crystallography. TBP belongs to a group of multisubunit enzymes that assist in transcribing RNA polymerases in eukaryotes. TBP from the plant Arabidopsis thaliana was found to be draped around the DNA molecule, with the DNA-binding fold held in a symmetric alpha-beta structure and with the DNA-binding surface consisting of a curved, antiparallel beta-sheet. This structure probably facilitates TBP in interacting with other transcription initiation factors and proteins.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
Article Abstract:
Max is a b/HLH/Z protein which heter-oligomerizes with Myc oncoproteins that authorizes them to link DNA. The helix-loop-helix (HLH) transcription factors feature a highly conserved bipartite DNA-binding region. The basic /helix-loop-helix/leucine zipper (b/HLH/Z) domain of Max knotted with DNA, has been viewed with X-ray crystallography. Max binds to CACGTG by direct contact of alpha-helical basic region and major groove. The structural description and refinements of DNA-binding domain, monomer structure, parallel four-helix bundle, leucine zipper and loop are discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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