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216 a.a.
_CA
Key reference
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.
Literature references that cite this PDB file's key reference
PubMed id Reference 19922791 T.M.Hansen, H.Singh, T.A.Tahir, and N.P.Brindle (2010).
Effects of angiopoietins-1 and -2 on the receptor tyrosine kinase Tie2 are differentially regulated at the endothelial cell surface.Cell Signal, 22, 527-532.
17322526 K.B.Pabbisetty, X.Yue, C.Li, J.P.Himanen, R.Zhou, D.B.Nikolov, and L.Hu (2007).
Kinetic analysis of the binding of monomeric and dimeric ephrins to Eph receptors: correlation to function in a growth cone collapse assay.Protein Sci, 16, 355-361.
17148457 M.Tanio, S.Kondo, S.Sugio, and T.Kohno (2007).
Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain.J Biol Chem, 282, 3889-3895.
PDB code: 2d39 16820685 M.Tanio, S.Kondo, S.Sugio, and T.Kohno (2006).
Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain.Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 652-655.
16645151 N.P.Brindle, P.Saharinen, and K.Alitalo (2006).
Signaling and functions of angiopoietin-1 in vascular protection.Circ Res, 98, 1014-1023.
16732286 W.A.Barton, D.Tzvetkova-Robev, E.P.Miranda, M.V.Kolev, K.R.Rajashankar, J.P.Himanen, and D.B.Nikolov (2006).
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.Nat Struct Mol Biol, 13, 524-532.
PDB codes: 2gy5 2gy7
16379598 S.G.Rockson (2005).
Literature watch. A genetic Xenopus laevis tadpole model to study lymphangiogenesis.Lymphat Res Biol, 3, 263-267. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
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