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.
CITATION STYLE
Barton, W. A., Tzvetkova, D., & Nikolov, D. B. (2005). Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition. Structure, 13(5), 825–832. https://doi.org/10.1016/j.str.2005.03.009
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