1Z3U: Structure Of The Angiopoietin-2 Recptor Binding Domain And Identification Of Surfaces Involved In Tie2 Recognition

Citation:
Abstract
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.
PDB ID: 1Z3UDownload
MMDB ID: 34278
PDB Deposition Date: 2005/3/14
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.25  Å
Source Organism:
Similar Structures:
Biological Unit for 1Z3U: monomeric; determined by author
Molecular Components in 1Z3U
Label Count Molecule
Protein (1 molecule)
1
Angiopoietin-2(Gene symbol: ANGPT2)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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