Crystal structure of the WD40 domain of human PRPF19

Biochem Biophys Res Commun. 2017 Nov 25;493(3):1250-1253. doi: 10.1016/j.bbrc.2017.09.145. Epub 2017 Sep 28.

Abstract

Human Pre-mRNA Processing factor 19 (hPRPF19) is an important component in human spliceosome machinery. hPRPF19 contains a WD40 repeats domain at its C-terminus, which is also conserved in yeast. Here we determined the crystal structure of the C-terminal WD40 repeat domain of hPRPF19 by X-ray crystallography. Our structural analysis revealed some significantly different structure features between the human and yeast Prp19 WD40 repeat domain. However, there are also conserved clusters of residues at the bottom surface of the fourth and the fifth WD40 repeats, which provides the important implication for the conserved Prp19 proteins in both human and yeast.

Keywords: Crystal structure; Human Pre-mRNA-processing factor 19 (hPRPF19); Spliceosome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • DNA Repair Enzymes / chemistry*
  • DNA Repair Enzymes / genetics
  • DNA Repair Enzymes / metabolism
  • Humans
  • Models, Molecular
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Protein Conformation
  • Protein Domains
  • RNA Splicing Factors / chemistry*
  • RNA Splicing Factors / genetics
  • RNA Splicing Factors / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • WD40 Repeats

Substances

  • Nuclear Proteins
  • PRP19 protein, S cerevisiae
  • RNA Splicing Factors
  • Saccharomyces cerevisiae Proteins
  • DNA Repair Enzymes
  • PRPF19 protein, human