Three-dimensional models of the oligomeric human asialoglycoprotein receptor (ASGP-R)

Int J Mol Sci. 2010 Oct 11;11(10):3867-84. doi: 10.3390/ijms11103867.

Abstract

The work presented here is aimed at suggesting plausible hypotheses for functional oligomeric forms of the human asialoglycoprotein receptor (ASGP-R), by applying a combination of different computational techniques. The functional ASGP-R is a hetero-oligomer, that comprises of several subunits of two different kinds (H1 and H2), which are highly homologous. Its stoichiometry is still unknown. An articulated step-wise modeling protocol was used in order to build the receptor model in a minimal oligomeric form, necessary for it to bind multi-antennary carbohydrate ligands. The ultimate target of the study is to contribute to increasing the knowledge of interactions between the human ASGP-R and carbohydrate ligands, at the molecular level, pertinent to applications in the field of hepatic tissue engineering.

Keywords: ASGP-R; antennary carbohydratic ligands; oligomeric form.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asialoglycoprotein Receptor / chemistry*
  • Binding Sites
  • Humans
  • Molecular Docking Simulation*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Tertiary

Substances

  • Asialoglycoprotein Receptor