Structure of IRF-1 with bound DNA reveals determinants of interferon regulation

Carlos R. Escalante, Junming Yie, Dimitris Thanos and Aneel K. Aggarwal ()
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Carlos R. Escalante: Structural Biology Program, Box 1677, Mount Sinai School of Medicine
Junming Yie: Columbia University
Dimitris Thanos: Columbia University
Aneel K. Aggarwal: Structural Biology Program, Box 1677, Mount Sinai School of Medicine

Nature, 1998, vol. 391, issue 6662, 103-106

Abstract: Abstract The family of interferon regulatory factor (IRF) transcription factors is important in the regulation of interferons in response to infection by virus and in the regulation of interferon-inducible genes1,2. The IRF family is characterized by a unique ‘tryptophan cluster’ DNA-binding region. Here we report the crystal structure of the IRF-1 region bound to the natural positive regulatory domain I (PRD I) DNA element from the interferon-β promoter1. The structure provides the first three-dimensional view of a member of the growing IRF family, revealing a new helix–turn–helix motif that latches onto DNA through three of the five conserved tryptophans. The motif selects a short GAAA core sequence through an obliquely angled recognition helix, with an accompanying bending of the DNA axis in the direction of the protein. Together, these features suggest a basis for the occurrence of GAAA repeats within IRF response elements and provide clues to the assembly of the higher-order interferon-β enhancesome.

Date: 1998
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DOI: 10.1038/34224

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