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Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

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  • Shiqian Qi

    (State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and National Collaborative Innovation Center
    University of California, Berkeley)

  • Zichong Li

    (University of California, Berkeley)

  • Ursula Schulze-Gahmen

    (University of California, Berkeley)

  • Goran Stjepanovic

    (University of California, Berkeley
    Lawrence Berkeley National Laboratory)

  • Qiang Zhou

    (University of California, Berkeley)

  • James H. Hurley

    (University of California, Berkeley
    Lawrence Berkeley National Laboratory)

Abstract

The intrinsically disordered scaffold proteins AFF1/4 and the transcription elongation factors ELL1/2 are core components of the super elongation complex required for HIV-1 proviral transcription. Here we report the 2.0-Å resolution crystal structure of the human ELL2 C-terminal domain bound to its 50-residue binding site on AFF4, the ELLBow. The ELL2 domain has the same arch-shaped fold as the tight junction protein occludin. The ELLBow consists of an N-terminal helix followed by an extended hairpin that we refer to as the elbow joint, and occupies most of the concave surface of ELL2. This surface is important for the ability of ELL2 to promote HIV-1 Tat-mediated proviral transcription. The AFF4–ELL2 interface is imperfectly packed, leaving a cavity suggestive of a potential binding site for transcription-promoting small molecules.

Suggested Citation

  • Shiqian Qi & Zichong Li & Ursula Schulze-Gahmen & Goran Stjepanovic & Qiang Zhou & James H. Hurley, 2017. "Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription," Nature Communications, Nature, vol. 8(1), pages 1-10, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14076
    DOI: 10.1038/ncomms14076
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