Sequence and structural difference favors a distinct preference of Wnt3a binding with co-receptor LRP6

J Biomol Struct Dyn. 2015;33(10):2133-44. doi: 10.1080/07391102.2014.991352. Epub 2015 Jan 6.

Abstract

Wnt signaling pathway plays a key role in a wide array of development and physiological processes. Wnt proteins interact with two different co-receptors LRP5/6 and ROR 2, leading to different signal transductions in the cell. Though the Wnt family of proteins has high sequence similarity the specificity for particular co-receptor is not well understood. The choice of pathway is attributed to the binding of Wnt complex to the co-receptor. Our current study is a novel approach using homology modeling, docking, and structural alignment to unravel the structural differences between Wnt3a and Wnt5b binding to LRP6. The conservation of a protruding loop has been identified in Wnt3a protein indicating an enhanced ability of Wnt3a to bind to LRP5/6 against its counter parts. The docking studies have further substantiated the findings. This could potentially help us design and develop novel inhibitors targeting Wnt3a-LRP6 complex in specific tissues or disease states.

Keywords: LRP6; Wnt3a; Wnt5a.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Humans
  • Hydrogen Bonding
  • Low Density Lipoprotein Receptor-Related Protein-6 / chemistry*
  • Molecular Docking Simulation*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Signal Transduction
  • Static Electricity
  • Structural Homology, Protein
  • Thermodynamics
  • Wnt Proteins / chemistry*
  • Wnt3A Protein / chemistry*

Substances

  • LRP6 protein, human
  • Low Density Lipoprotein Receptor-Related Protein-6
  • WNT3A protein, human
  • WNT5B protein, human
  • Wnt Proteins
  • Wnt3A Protein