2GY5
Tie2 Ligand-Binding Domain Crystal Structure
Summary for 2GY5
| Entry DOI | 10.2210/pdb2gy5/pdb |
| Related | 2gy7 |
| Descriptor | Angiopoietin-1 receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | ligand-binding domain, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: Q02763 |
| Total number of polymer chains | 1 |
| Total formula weight | 48676.44 |
| Authors | Barton, W.A.,Nikolov, D.B. (deposition date: 2006-05-09, release date: 2006-06-06, Last modification date: 2024-10-30) |
| 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 Cited by 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: 16732286DOI: 10.1038/nsmb1101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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