2WO2
Crystal Structure of the EphA4-ephrinB2 complex
Summary for 2WO2
Entry DOI | 10.2210/pdb2wo2/pdb |
Related | 2VSK 2VSM 2WO1 2WO3 |
Descriptor | EPHRIN TYPE-A RECEPTOR, EPHRIN-B2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | transferase-signaling protein complex, osteogenesis, axon guidance, cell surface receptor, developmental protein, neurogenesis, cell signaling, transferase/signaling protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 39195.25 |
Authors | Bowden, T.A.,Aricescu, A.R.,Nettleship, J.E.,Siebold, C.,Rahman-Huq, N.,Owens, R.J.,Stuart, D.I.,Jones, E.Y. (deposition date: 2009-07-21, release date: 2009-10-27, Last modification date: 2023-12-20) |
Primary citation | Bowden, T.A.,Aricescu, A.R.,Nettleship, J.E.,Siebold, C.,Rahman-Huq, N.,Owens, R.J.,Stuart, D.I.,Jones, E.Y. Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin Signalling Structure, 17:1386-, 2009 Cited by PubMed Abstract: The EphA4 tyrosine kinase cell surface receptor regulates an array of physiological processes and is the only currently known class A Eph receptor that binds both A and B class ephrins with high affinity. We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with (1) ephrinB2 and (2) ephrinA2. This set of structures shows that EphA4 has significant conformational plasticity in its ligand binding face. In vitro binding data demonstrate that it has a higher affinity for class A than class B ligands. Structural analyses, drawing on previously reported Eph receptor structures, show that EphA4 in isolation and in complex with ephrinA2 resembles other class A Eph receptors but on binding ephrinB2 assumes structural hallmarks of the class B Eph receptors. This interactive plasticity reveals EphA4 as a structural chameleon, able to adopt both A and B class Eph receptor conformations, and thus provides a molecular basis for EphA-type cross-class reactivity. PubMed: 19836338DOI: 10.1016/J.STR.2009.07.018 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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