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PDBsum entry 3mx0

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Transferase receptor/signalling protein PDB id
3mx0
Contents
Protein chains
406 a.a.
138 a.a.
Ligands
NAG-NAG-NAG ×2
NAG ×2

References listed in PDB file
Key reference
Title Architecture of eph receptor clusters.
Authors J.P.Himanen, L.Yermekbayeva, P.W.Janes, J.R.Walker, K.Xu, L.Atapattu, K.R.Rajashankar, A.Mensinga, M.Lackmann, D.B.Nikolov, S.Dhe-Paganon.
Ref. Proc Natl Acad Sci U S A, 2010, 107, 10860-10865.
PubMed id 20505120
Abstract
Eph receptor tyrosine kinases and their ephrin ligands regulate cell navigation during normal and oncogenic development. Signaling of Ephs is initiated in a multistep process leading to the assembly of higher-order signaling clusters that set off bidirectional signaling in interacting cells. However, the structural and mechanistic details of this assembly remained undefined. Here we present high-resolution structures of the complete EphA2 ectodomain and complexes with ephrin-A1 and A5 as the base unit of an Eph cluster. The structures reveal an elongated architecture with novel Eph/Eph interactions, both within and outside of the Eph ligand-binding domain, that suggest the molecular mechanism underlying Eph/ephrin clustering. Structure-function analysis, by using site-directed mutagenesis and cell-based signaling assays, confirms the importance of the identified oligomerization interfaces for Eph clustering.
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