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2WO2

Crystal Structure of the EphA4-ephrinB2 complex

Summary for 2WO2
Entry DOI10.2210/pdb2wo2/pdb
Related2VSK 2VSM 2WO1 2WO3
DescriptorEPHRIN TYPE-A RECEPTOR, EPHRIN-B2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordstransferase-signaling protein complex, osteogenesis, axon guidance, cell surface receptor, developmental protein, neurogenesis, cell signaling, transferase/signaling protein
Biological sourceHomo sapiens (Human)
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Total number of polymer chains2
Total formula weight39195.25
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 citationBowden, 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: 19836338
DOI: 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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