Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition

  • Barton W
  • Tzvetkova D
  • Nikolov D
  • 54

    Readers

    Mendeley users who have this article in their library.
  • 39

    Citations

    Citations of this article.

Abstract

The angiopoietins comprise a small class of secreted glycoproteins that play crucial roles in the maturation and maintenance of the mammalian vascular and lymphatic systems. They exert their effects through a member of the tyrosine kinase receptor family, Tie2. Angiopoietin/Tie2 signaling is unique among tyrosine kinase receptor-ligand systems in that distinct angiopoietin ligands, although highly homologous, can function as agonists or antagonists in a context-dependent manner. In an effort to understand this molecular dichotomy, we have crystallized and determined the 2.4 Å crystal structure of the Angiopoietin-2 (Ang2) receptor binding region. The structure reveals a fibrinogen fold with a unique C-terminal P domain. Conservation analysis and structure-based mutagenesis identify a groove on the Ang2 molecular surface that mediates receptor recognition. ©2005 Elsevier Ltd All rights reserved.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text

Authors

  • William A. Barton

  • Dorothea Tzvetkova

  • Dimitar B. Nikolov

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free