1z3s
From Proteopedia
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'''Angiopoietin-2 Receptor Binding Domain''' | '''Angiopoietin-2 Receptor Binding Domain''' | ||
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[[Category: Nikolov, D B.]] | [[Category: Nikolov, D B.]] | ||
[[Category: Tzvetkova, D.]] | [[Category: Tzvetkova, D.]] | ||
| - | [[Category: | + | [[Category: Angiogenesis]] |
| - | [[Category: | + | [[Category: Tie2 binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:08:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:08, 3 May 2008
Angiopoietin-2 Receptor Binding Domain
Overview
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.
About this Structure
1Z3S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition., Barton WA, Tzvetkova D, Nikolov DB, Structure. 2005 May;13(5):825-32. PMID:15893672 Page seeded by OCA on Sat May 3 17:08:58 2008
