Structure of the HECT domain of human WWP2

Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1251-7. doi: 10.1107/S2053230X1501554X. Epub 2015 Sep 23.

Abstract

WWP2 is a HECT-domain ubiquitin ligase of the Nedd4 family, which is involved in various important biological processes, such as protein degradation, membrane-protein sorting and transportation, the immune response, pluripotency of embryonic stem cells, tumourigenesis and metastasis. The HECT domain provides the intrinsic ubiquitin ligase activity of WWP2. Here, the expression, purification, crystallization and crystallographic analysis of the HECT domain of human WWP2 (HECT(WWP2)) are reported. HECT(WWP2) has been crystallized and the crystals diffracted to 2.50 Å resolution. They belonged to space group P41212 and the structure has been solved via molecular replacement. The overall structure of HECT(WWP2) has an inverted T-shape. This structure displays a high degree of conservation with previously published structures of Nedd4 subfamily members.

Keywords: HECT domain; WWP2; crystal structure; ubiquitin ligase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Endosomal Sorting Complexes Required for Transport / chemistry
  • Humans
  • Nedd4 Ubiquitin Protein Ligases
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Structural Homology, Protein
  • Ubiquitin-Protein Ligases / chemistry*

Substances

  • Endosomal Sorting Complexes Required for Transport
  • Nedd4 Ubiquitin Protein Ligases
  • Nedd4 protein, human
  • WWP2 protein, human
  • Ubiquitin-Protein Ligases

Associated data

  • PDB/4Y07