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Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding

Gajiwala, K. S.
Chen, H.
Cornille, F.
Roques, B. P.
Burley, S. K.
Published in Nature. 2000, vol. 403, no. 6772, p. 916-921
Abstract Regulatory factor X (RFX) proteins are transcriptional activators that recognize X-boxes (DNA of the sequence 5'-GTNRCC(0-3N)RGYAAC-3', where N is any nucleotide, R is a purine and Y is a pyrimidine) using a highly conserved 76-residue DNA-binding domain (DBD). DNA-binding defects in the protein RFX5 cause bare lymphocyte syndrome or major histocompatibility antigen class II deficiency. RFX1, -2 and -3 regulate expression of other medically important gene products (for example, interleukin-5 receptor alpha chain, IL-5R alpha). Fusions of the ligand-binding domain of the oestrogen receptor with the DBD of RFX4 occur in some human breast tumours. Here we present a 1.5 A-resolution structure of two copies of the DBD of human RFX1 (hRFX1) binding cooperatively to a symmetrical X-box. hRFX1 is an unusual member of the winged-helix subfamily of helix-turn-helix proteins because it uses a beta-hairpin (or wing) to recognize DNA instead of the recognition helix typical of helix-turn-helix proteins. A new model for interactions between linker histones and DNA is proposed.
Keywords Amino Acid SequenceBinding SitesCrystallography, X-RayDNA/ chemistry/metabolismDNA-Binding Proteins/ chemistry/metabolismElectrochemistryHelix-Turn-Helix MotifsHumansModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationProtein Structure, SecondaryTranscription Factors/ chemistry/metabolism
PMID: 10706293
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GAJIWALA, K. S. et al. Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. In: Nature, 2000, vol. 403, n° 6772, p. 916-921. doi: 10.1038/35002634 https://archive-ouverte.unige.ch/unige:11265

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Deposited on : 2010-08-27

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