Crystal structure of the FAS1 domain of the hyaluronic acid receptor stabilin-2

Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):695-701. doi: 10.1107/S2059798318007271. Epub 2018 Jun 27.

Abstract

Recent research has identified a potential role of the hyaluronic acid receptor stabilin-2 (Stab2) in cancer metastasis. Stab2 belongs to a group of scavenger receptors and is responsible for the clearance of more than ten ligands, including hyaluronic acid (HA). In vivo experiments on mice have shown that the absence of Stab2, or its blocking by an antibody, effectively opposes cancer metastasis, which is accompanied by an increase in the level of circulating HA. Knowledge of ligand recognition and signal transduction by Stab2 is limited and no three-dimensional structures of any protein fragments of this receptor have been solved to date. Here, a high-resolution X-ray structure of the seventh FAS1 domain of Stab2 is reported. This structure provides the first insight into the Stab2 structure.

Keywords: NMR; Stab2; X-ray crystallography; hyaluronic acid receptor; stabilin-2 FAS1 domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion Molecules, Neuronal / chemistry*
  • Crystallography, X-Ray
  • Hyaluronic Acid
  • Mice
  • Protein Conformation
  • Protein Domains
  • Signal Transduction
  • fas Receptor / chemistry*

Substances

  • Cell Adhesion Molecules, Neuronal
  • Stab2 protein, mouse
  • fas Receptor
  • Hyaluronic Acid