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1z3u
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(New page: 200px<br /> <applet load="1z3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z3u, resolution 2.25Å" /> '''Structure of the An...)
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Revision as of 18:22, 12 November 2007
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Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition
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
1Z3U is a Single protein structure of sequence from Homo sapiens with CA as ligand. 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 Mon Nov 12 20:28:59 2007
