1z3s: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
caption="1z3s, resolution 2.35&Aring;" />
caption="1z3s, resolution 2.35&Aring;" />
'''Angiopoietin-2 Receptor Binding Domain'''<br />
'''Angiopoietin-2 Receptor Binding Domain'''<br />


==Overview==
==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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z3S OCA].  
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.A.]]
[[Category: Barton, W A.]]
[[Category: Nikolov, D.B.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:28:56 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:49 2008''

Revision as of 17:11, 21 February 2008

File:1z3s.gif


1z3s, resolution 2.35Å

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Angiopoietin-2 Receptor Binding Domain

OverviewOverview

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 StructureAbout this Structure

1Z3S is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 16:11:49 2008

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