Bacterial expression and preliminary crystallographic studies of a 149-residue fragment of human Caprin-1

Acta Crystallogr F Struct Biol Commun. 2015 Mar;71(Pt 3):324-9. doi: 10.1107/S2053230X15002642. Epub 2015 Feb 19.

Abstract

Caprin-1 is an RNA-binding protein which plays critical roles in several important biological processes, including cellular proliferation, the interferon-mediated antiviral innate immune response, the maintenance of synaptic plasticity and the formation of RNA stress granules. Caprin-1 has been implicated in the pathogenesis of several human diseases, including osteosarcoma, breast cancer, viral infections, hearing loss and neurodegenerative disorders. Despite the emerging biological and physiopathological significance of Caprin-1, no structural information is available for this protein. Moreover, Caprin-1 does not have sequence similarity to any other protein with a known structure. It is therefore expected that structural studies will play a particularly crucial role in revealing the functional mechanisms of Caprin-1. Here, a protein fragment of human Caprin-1 consisting of residues 112-260 was expressed, purified and crystallized. Native and Se-SAD data sets were collected to resolutions to 2.05 and 2.65 Å, respectively, in different space groups.

Keywords: Caprin-1; Caprin-2; DENV-2 sfRNA; G3BP1; JEV core protein; Pou4f3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / biosynthesis
  • Cell Cycle Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Gene Expression
  • Peptide Fragments / biosynthesis
  • Peptide Fragments / chemistry

Substances

  • CAPRIN1 protein, human
  • Cell Cycle Proteins
  • Peptide Fragments