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


Authors: Barton, W. A.; Tzvetkova, D.; Nikolov, D. B.
Article Title: Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition
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.
Keywords: controlled study; human cell; mutation; protein domain; mammalia; carboxy terminal sequence; calcium; amino acid sequence; molecular sequence data; molecular recognition; crystal structure; protein structure, tertiary; binding sites; protein structure; crystallization; angiopoietin receptor; receptor, tie-2; mutagenesis; crystallography
Journal Title: Structure
Volume: 13
Issue: 5
ISSN: 0969-2126
Publisher: Cell Press  
Date Published: 2005-05-01
Start Page: 825
End Page: 832
Language: English
DOI: 10.1016/j.str.2005.03.009
PUBMED: 15893672
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 18" - "Export Date: 24 October 2012" - "CODEN: STRUE" - "Source: Scopus"
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  1. William A Barton
    17 Barton
  2. Dimitar B Nikolov
    86 Nikolov
  3. Dorothea Dimitrova Robev
    16 Robev