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PDBsum entry 2x10
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Contents |
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* Residue conservation analysis
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PDB id:
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Receptor
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Title:
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Crystal structure of the complete epha2 ectodomain
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Structure:
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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
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_variant: gnti-deficient. Expression_system_cell_line: hek293.
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Resolution:
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3.00Å
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R-factor:
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0.239
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R-free:
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0.299
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Authors:
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E.Seiradake,K.Harlos,G.Sutton,A.R.Aricescu,E.Y.Jones
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Key ref:
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E.Seiradake
et al.
(2010).
An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly.
Nat Struct Biol,
17,
398-402.
PubMed id:
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Date:
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21-Dec-09
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Release date:
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16-Mar-10
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PROCHECK
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Headers
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References
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P29317
(EPHA2_HUMAN) -
Ephrin type-A receptor 2 from Homo sapiens
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Seq:
Struc:
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976 a.a.
485 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.7.10.1
- receptor protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
Bound ligand (Het Group name = )
matches with 41.38% similarity
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Nat Struct Biol
17:398-402
(2010)
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PubMed id:
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An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly.
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E.Seiradake,
K.Harlos,
G.Sutton,
A.R.Aricescu,
E.Y.Jones.
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ABSTRACT
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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.
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Links
