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PDBsum entry 3mx0
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Transferase receptor/signalling protein
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PDB id
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3mx0
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase receptor/signalling protein
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Title:
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Crystal structure of epha2 ectodomain in complex with ephrin-a5
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Structure:
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Ephrin type-a receptor 2. Chain: a, c. Fragment: ectodomain (unp residues 27-435). Synonym: tyrosine-protein kinase receptor eck, epithelial cell kinase. Engineered: yes. Ephrin-a5. Chain: b, d. Fragment: ectodomain (unp residues 28-165).
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: epha2, eck. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek-293. Gene: efna5, eplg7, lerk7.
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Resolution:
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3.51Å
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R-factor:
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0.237
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R-free:
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0.295
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Authors:
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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
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Key ref:
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J.P.Himanen
et al.
(2010).
Architecture of Eph receptor clusters.
Proc Natl Acad Sci U S A,
107,
10860-10865.
PubMed id:
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Date:
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06-May-10
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Release date:
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30-Jun-10
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, C:
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
Bound ligand (Het Group name = )
matches with 47.62% similarity
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=
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O-phospho-L-tyrosyl-[protein]
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+
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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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Proc Natl Acad Sci U S A
107:10860-10865
(2010)
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PubMed id:
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Architecture of Eph receptor clusters.
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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.
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ABSTRACT
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Brasch,
O.J.Harrison,
G.Ahlsen,
S.M.Carnally,
R.M.Henderson,
B.Honig,
and
L.Shapiro
(2011).
Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.
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J Mol Biol,
408,
57-73.
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PDB code:
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N.Singla,
H.Erdjument-Bromage,
J.P.Himanen,
T.W.Muir,
and
D.B.Nikolov
(2011).
A semisynthetic Eph receptor tyrosine kinase provides insight into ligand-induced kinase activation.
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Chem Biol,
18,
361-371.
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I.Bethani,
S.S.Skånland,
I.Dikic,
and
A.Acker-Palmer
(2010).
Spatial organization of transmembrane receptor signalling.
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EMBO J,
29,
2677-2688.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
