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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 2.25&Aring;" /> '''Structure of the An...)
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[[Image:1z3u.gif|left|200px]]<br />
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[[Image:1z3u.gif|left|200px]]<br /><applet load="1z3u" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1z3u" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1z3u, resolution 2.25&Aring;" />
caption="1z3u, resolution 2.25&Aring;" />
'''Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition'''<br />
'''Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition'''<br />
==Overview==
==Overview==
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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.
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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==
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1Z3U 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=1Z3U OCA].
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1Z3U 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=1Z3U OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barton, W.A.]]
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[[Category: Barton, W A.]]
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[[Category: Nikolov, D.B.]]
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[[Category: Nikolov, D B.]]
[[Category: Tzvetkova, D.]]
[[Category: Tzvetkova, D.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: tie2 binding]]
[[Category: tie2 binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:28:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:50 2008''

Revision as of 14:11, 21 February 2008


1z3u, resolution 2.25Å

Drag the structure with the mouse to rotate

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 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 Thu Feb 21 16:11:50 2008

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