1z3u
From Proteopedia
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| - | [[Image:1z3u.gif|left|200px]] | + | [[Image:1z3u.gif|left|200px]] |
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| - | '''Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition''' | + | {{Structure |
| + | |PDB= 1z3u |SIZE=350|CAPTION= <scene name='initialview01'>1z3u</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z3U is a [ | + | 1Z3U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3U OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15893672 15893672] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tie2 binding]] | [[Category: tie2 binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:56 2008'' |
Revision as of 13:30, 20 March 2008
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| , resolution 2.25Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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