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Cell adhesion/immunue system
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PDB id
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3ff7
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Contents |
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* Residue conservation analysis
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PDB id:
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Cell adhesion/immunue system
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Title:
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Structure of nk cell receptor klrg1 bound to e-cadherin
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Structure:
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Epithelial cadherin. Chain: a, b. Fragment: unp residues 155-253, cadherin 1 domain. Synonym: e-cadherin, cadherin-1, uvomorulin, cam 120/80, e- cad/ctf1, e-cad/ctf2, e-cad/ctf3. Engineered: yes. Mutation: yes. Killer cell lectin-like receptor subfamily g member 1.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cdh1, cdhe, uvo. Expressed in: escherichia coli. Gene: klrg1, clec15a, mafa, mafal. Expressed in: escherichia coli
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Resolution:
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1.80Å
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R-factor:
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0.214
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R-free:
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0.246
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Authors:
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Y.Li,R.A.Mariuzza
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Key ref:
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Y.Li
et al.
(2009).
Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.
Immunity,
31,
35-46.
PubMed id:
DOI:
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Date:
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02-Dec-08
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Release date:
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28-Jul-09
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PROCHECK
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Headers
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References
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P12830
(CADH1_HUMAN) -
Cadherin-1
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Seq:
Struc:
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882 a.a.
97 a.a.*
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Gene Ontology (GO) functional annotation
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Cellular component
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membrane
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1 term
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Biological process
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homophilic cell adhesion
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1 term
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Biochemical function
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binding
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2 terms
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DOI no:
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Immunity
31:35-46
(2009)
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PubMed id:
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Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.
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Y.Li,
M.Hofmann,
Q.Wang,
L.Teng,
L.K.Chlewicki,
H.Pircher,
R.A.Mariuzza.
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ABSTRACT
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The cytolytic activity of natural killer (NK) cells is regulated by inhibitory
receptors that detect the absence of self molecules on target cells. Structural
studies of missing self recognition have focused on NK receptors that bind MHC.
However, NK cells also possess inhibitory receptors specific for non-MHC
ligands, notably cadherins, which are downregulated in metastatic tumors. We
determined the structure of killer cell lectin-like receptor G1 (KLRG1) in
complex with E-cadherin. KLRG1 mediates missing self recognition by binding to a
highly conserved site on classical cadherins, enabling it to monitor expression
of several cadherins (E-, N-, and R-) on target cells. This site overlaps the
site responsible for cell-cell adhesion but is distinct from the integrin
alpha(E)beta(7) binding site. We propose that E-cadherin may coengage KLRG1 and
alpha(E)beta(7) and that KLRG1 overcomes its exceptionally weak affinity for
cadherins through multipoint attachment to target cells, resulting in inhibitory
signaling.
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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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C.Gründemann,
S.Schwartzkopff,
M.Koschella,
O.Schweier,
C.Peters,
D.Voehringer,
and
H.Pircher
(2010).
The NK receptor KLRG1 is dispensable for virus-induced NK and CD8+ T-cell differentiation and function in vivo.
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Eur J Immunol, 40,
1303-1314.
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H.P.Su,
K.Singh,
A.G.Gittis,
and
D.N.Garboczi
(2010).
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.
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J Virol, 84,
2502-2510.
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PDB code:
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S.Jonjic
(2010).
Functional plasticity and robustness are essential characteristics of biological systems: lessons learned from KLRG1-deficient mice.
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Eur J Immunol, 40,
1241-1243.
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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
