2gy7
Angiopoietin-2/Tie2 Complex Crystal Structure
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Venous malformations, multiple cutaneous and mucosal OMIM:[600221]
About this StructureAbout this Structure
2GY7 is a Protein complex structure of sequences from Homo sapiens with NAG, CA and SO4 as ligands. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex., Barton WA, Tzvetkova-Robev D, Miranda EP, Kolev MV, Rajashankar KR, Himanen JP, Nikolov DB, Nat Struct Mol Biol. 2006 Jun;13(6):524-32. Epub 2006 May 28. PMID:16732286
Page seeded by OCA on Mon Nov 12 22:23:44 2007