PMID: 19836338

 

    Legend: Gene, Sites

Title : Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling

Abstract :

1. 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
2. We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with ( 1) ephrinB2 and ( 2) ephrinA2
3. This set of structures shows that EphA4 has significant conformational plasticity in its ligand binding face
4. In vitro binding data demonstrate that it has a higher affinity for class A than class B ligands
5. 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
6. 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

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

• 2. structure of the EphA4, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
Eph receptor	2041	1,5,6
2) ephrinA2	1943	2
eph receptor A4	2043	0
EphA4	2043	1,3,5,6
ephrinB2	1948	5
Eph receptors	2041	5
1) ephrinB2	1948	2
cell surface receptor	57126	1
ephrinA2	1943	5
structure of the EphA4	2043	2