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1Z3S

Angiopoietin-2 Receptor Binding Domain

Summary for 1Z3S
Entry DOI10.2210/pdb1z3s/pdb
Related1Z3U
DescriptorAngiopoietin-2, CALCIUM ION (3 entities in total)
Functional Keywordsangiogenesis, tie2 binding, signaling protein
Biological sourceHomo sapiens (human)
Cellular locationSecreted: O15123
Total number of polymer chains2
Total formula weight49879.53
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 citationBarton, 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: 15893672
DOI: 10.1016/j.str.2005.03.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

237735

数据于2025-06-18公开中

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