2GY7

Angiopoietin-2/Tie2 Complex Crystal Structure

Summary for 2GY7

• Entry DOI: 10.2210/pdb2gy7/pdb
• Related: 1Z3S 2GY5
• Descriptor: Angiopoietin-2, Angiopoietin-1 receptor, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: receptor-ligand complex, signaling protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 74071.66

Authors

Barton, W.A.,Nikolov, D.B. (deposition date: 2006-05-09, release date: 2006-06-06, Last modification date: 2024-12-25)

Primary citation

Barton, W.A.,Tzvetkova-Robev, D.,Miranda, E.P.,Kolev, M.V.,Rajashankar, K.R.,Himanen, J.P.,Nikolov, D.B.
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
Nat.Struct.Mol.Biol., 13:524-532, 2006

PubMed Abstract: The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2. In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2 binds at the tip of the arrowhead utilizing a lock-and-key mode of ligand recognition-unique for a receptor kinase-where two complementary surfaces interact with each other with no domain rearrangements and little conformational change in either molecule. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. Analysis of the structures and structure-based mutagenesis provide insight into the mechanism of receptor activation and support the hypothesis that all angiopoietins interact with Tie2 in a structurally similar manner.

PubMed: 16732286
DOI: 10.1038/nsmb1101

Experimental method

X-RAY DIFFRACTION (3.7 Å)