1z3s
From Proteopedia
(New page: 200px<br /> <applet load="1z3s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z3s, resolution 2.35Å" /> '''Angiopoietin-2 Rece...) |
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| - | [[Image:1z3s.gif|left|200px]]<br /> | + | [[Image:1z3s.gif|left|200px]]<br /><applet load="1z3s" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1z3s" size=" | + | |
caption="1z3s, resolution 2.35Å" /> | caption="1z3s, resolution 2.35Å" /> | ||
'''Angiopoietin-2 Receptor Binding Domain'''<br /> | '''Angiopoietin-2 Receptor Binding Domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The angiopoietins comprise a small class of secreted glycoproteins that | + | 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== | ==About this Structure== | ||
| - | 1Z3S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Z3S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barton, W | + | [[Category: Barton, W A.]] |
| - | [[Category: Nikolov, D | + | [[Category: Nikolov, D B.]] |
[[Category: Tzvetkova, D.]] | [[Category: Tzvetkova, D.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: tie2 binding]] | [[Category: tie2 binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:49 2008'' |
Revision as of 14:11, 21 February 2008
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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 with 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
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