1Z3S
Angiopoietin-2 Receptor Binding Domain
Summary for 1Z3S
Entry DOI | 10.2210/pdb1z3s/pdb |
Related | 1Z3U |
Descriptor | Angiopoietin-2, CALCIUM ION (3 entities in total) |
Functional Keywords | angiogenesis, tie2 binding, signaling protein |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: O15123 |
Total number of polymer chains | 2 |
Total formula weight | 49879.53 |
Authors | Barton, W.A.,Tzvetkova, D.,Nikolov, D.B. (deposition date: 2005-03-14, release date: 2005-07-12, Last modification date: 2024-10-30) |
Primary citation | Barton, W.A.,Tzvetkova, D.,Nikolov, D.B. Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition. Structure, 13:825-832, 2005 Cited by PubMed 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 A 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. PubMed: 15893672DOI: 10.1016/j.str.2005.03.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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