spacer
spacer

PDBsum entry 2x10

Go to PDB code: 
protein ligands metals links
Receptor PDB id
2x10
Jmol
Contents
Protein chain
485 a.a. *
Ligands
NAG
Metals
_CL
* Residue conservation analysis
PDB id:
2x10
Name: Receptor
Title: Crystal structure of the complete epha2 ectodomain
Structure: Ephrin type-a receptor 2. Chain: a. Fragment: ectodomain, residues 27-534. Synonym: tyrosine-protein kinase receptor eck, epithelial cell kinase, epha2. Engineered: yes. Other_details: NAG on asn407, di-methylation of lysines
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293.
Resolution:
3.00Å     R-factor:   0.238     R-free:   0.298
Authors: E.Seiradake,K.Harlos,G.Sutton,A.R.Aricescu,E.Y.Jones
Key ref: E.Seiradake et al. (2010). An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly. Nat Struct Mol Biol, 17, 398-402. PubMed id: 20228801
Date:
21-Dec-09     Release date:   16-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29317  (EPHA2_HUMAN) -  Ephrin type-A receptor 2
Seq:
Struc:
 
Seq:
Struc:
976 a.a.
485 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+
[protein]-L-tyrosine
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity
= ADP
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   1 term 
  Biological process     transmembrane receptor protein tyrosine kinase signaling pathway   3 terms 
  Biochemical function     ATP binding     2 terms  

 

 
    reference    
 
 
Nat Struct Mol Biol 17:398-402 (2010)
PubMed id: 20228801  
 
 
An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly.
E.Seiradake, K.Harlos, G.Sutton, A.R.Aricescu, E.Y.Jones.
 
  ABSTRACT  
 
Erythropoetin-producing hepatoma (Eph) receptors are cell-surface protein tyrosine kinases mediating cell-cell communication. Upon activation, they form signaling clusters. We report crystal structures of the full ectodomain of human EphA2 (eEphA2) both alone and in complex with the receptor-binding domain of the ligand ephrinA5 (ephrinA5 RBD). Unliganded eEphA2 forms linear arrays of staggered parallel receptors involving two patches of residues conserved across A-class Ephs. eEphA2-ephrinA5 RBD forms a more elaborate assembly, whose interfaces include the same conserved regions on eEphA2, but rearranged to accommodate ephrinA5 RBD. Cell-surface expression of mutant EphA2s showed that these interfaces are critical for localization at cell-cell contacts and activation-dependent degradation. Our results suggest a 'nucleation' mechanism whereby a limited number of ligand-receptor interactions 'seed' an arrangement of receptors which can propagate into extended signaling arrays.