PDBsum entry: 1z3u

Signaling protein

PDB id: 1z3u

Contents

Protein chains

216 a.a. *

Metals

_CA ×4

Waters ×379

* Residue conservation analysis

PDB id:

1z3u

Name:

Signaling protein

Title:

Structure of the angiopoietin-2 recptor binding domain and identification of surfaces involved in tie2 recognition

Structure:

Angiopoietin-2. Chain: a, b, c, d. Fragment: receptor binding domain (residues 281-496). Synonym: ang-2. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.25Å R-factor: 0.246 R-free: 0.278

Authors:

W.A.Barton,D.Tzvetkova,D.B.Nikolov

Key ref:

W.A.Barton et al. (2005). Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition. Structure, 13, 825-832. PubMed id: 15893672 DOI: 10.1016/j.str.2005.03.009

Date:

14-Mar-05 Release date: 12-Jul-05

Protein chains

O15123  (ANGP2_HUMAN) -  Angiopoietin-2

Seq: 496 a.a.

Struc: 216 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular space (1 term)
• Biological process: signal transduction (1 term)
• Biochemical function: receptor binding (1 term)

DOI no: 10.1016/j.str.2005.03.009

Structure 13:825-832 (2005)

PubMed id: 15893672

Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition.

W.A.Barton, D.Tzvetkova, D.B.Nikolov.

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.

Selected figure(s)

Figure 5.
Figure 5. Structure of the F468A/Y474A/Y475A Ang2-RBD Mutant
The structure is (blue) superimposed on the structure of the wild-type protein (red). Mutated residues are shown in yellow ball-and-stick format.

The above figure is reprinted by permission from Cell Press: Structure (2005, 13, 825-832) copyright 2005.

Figure was selected by an automated process.