Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK

Biochem Biophys Res Commun. 2020 Feb 26;523(1):263-266. doi: 10.1016/j.bbrc.2019.12.059. Epub 2019 Dec 19.

Abstract

RFX7 is an important member in the RFX family of DNA binding proteins and plays critical roles in natural killer cell-mediated immunity and neuron development. Our previous work identified ANKRA2 and RFXANK as the potential binding partners of RFX7. Here we present two structures of a RFX7 fragment, with one bound with the ANKRA2 ankyrin domain and the other bound to the RFXANK ankyrin domain. Our structural analysis reveals that both ANKRA2 and RFXANK recognize the PXLPXL motif of RFX7 and its flanking sequences via extensive hydrophobic interactions. Detailed structural comparison also provides an explanation for the different RFX7 binding affinities of ANKRA2 and RFXANK. Thus our work would provide clue to the understanding the roles of ANKRA2 and RFXANK in the RFX7-associated signaling pathway.

Keywords: Ankyrin repeats; Crystallography; Protein-protein interaction; Structural biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ankyrins / chemistry*
  • Ankyrins / metabolism*
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Protein Conformation
  • Regulatory Factor X Transcription Factors / chemistry*
  • Regulatory Factor X Transcription Factors / genetics
  • Regulatory Factor X Transcription Factors / metabolism*
  • Signal Transduction
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism*

Substances

  • ANKRA2 protein, human
  • Ankyrins
  • DNA-Binding Proteins
  • RFXANK protein, human
  • Regulatory Factor X Transcription Factors
  • Transcription Factors