Crystal structure of the WD40 domain of human PLRG1

Biochem Biophys Res Commun. 2021 Jan 1:534:474-477. doi: 10.1016/j.bbrc.2020.11.057. Epub 2020 Nov 22.

Abstract

PLRG1 is a evolutionarily conserved protein in spliceosome and plays an important role in maintaining the integral part of the splicoeosme and its proper splicing. Here we solved the high resolution crystal structure of the WD40 domain of human PLRG1 by crystallography and compared our crystal structure with the cryo-EM structure of PLRG1 bound with other splicing factors. We found that two loops of the WD40 domain become resolved upon binding to the proteins within the spliceosome. Thus our work characterize the dynamic property of PLRG1 during the spliceosome assembly by presenting its apo structure.

Keywords: Spliceosome; The nineteen complex; WD40 repeats; X-ray crystallography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Humans
  • Intracellular Signaling Peptides and Proteins / chemistry*
  • Models, Molecular
  • Nuclear Proteins / chemistry*
  • Protein Domains
  • WD40 Repeats

Substances

  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • PLRG1 protein, human