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PDBsum entry 3wyr
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Immune system
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PDB id
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3wyr
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PDB id:
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| Name: |
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Immune system
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Title:
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Crystal structure of killer cell immunoglobulin-like receptor 2dl4
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Structure:
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Killer cell immunoglobulin-like receptor 2dl4. Chain: a, b. Fragment: extracellular domain, unp residues 24-218. Synonym: cd158 antigen-like family member d, g9p, killer cell inhibitory receptor 103as, kir-103as, mhc class i nk cell receptor kir103as. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: kir2dl4, cd158d, kir103as. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293s.
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Resolution:
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2.80Å
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R-factor:
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0.212
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R-free:
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0.243
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Authors:
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J.P.Vivian,S.Moradi,J.Rossjohn
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Key ref:
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S.Moradi
et al.
(2015).
The structure of the atypical killer cell immunoglobulin-like receptor, KIR2DL4.
J Biol Chem,
290,
10460-10471.
PubMed id:
DOI:
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Date:
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07-Sep-14
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Release date:
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18-Mar-15
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PROCHECK
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Headers
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References
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Q99706
(KI2L4_HUMAN) -
Killer cell immunoglobulin-like receptor 2DL4 from Homo sapiens
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Seq:
Struc:
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377 a.a.
189 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 2 residue positions (black
crosses)
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DOI no:
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J Biol Chem
290:10460-10471
(2015)
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PubMed id:
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The structure of the atypical killer cell immunoglobulin-like receptor, KIR2DL4.
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S.Moradi,
R.Berry,
P.Pymm,
C.Hitchen,
S.A.Beckham,
M.C.Wilce,
N.G.Walpole,
C.S.Clements,
H.H.Reid,
M.A.Perugini,
A.G.Brooks,
J.Rossjohn,
J.P.Vivian.
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ABSTRACT
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The engagement of natural killer cell immunoglobulin-like receptors (KIRs) with
their target ligands, human leukocyte antigen (HLA) molecules, is a critical
component of innate immunity. Structurally, KIRs typically have either two
(D1-D2) or three (D0-D1-D2) extracellular immunoglobulin domains, with the D1
and D2 domain recognizing the α1 and α2 helices of HLA, respectively, whereas
the D0 domain of the KIR3DLs binds a loop region flanking the α1 helix of the
HLA molecule. KIR2DL4 is distinct from other KIRs (except KIR2DL5) in that it
does not contain a D1 domain and instead has a D0-D2 arrangement. Functionally,
KIR2DL4 is also atypical in that, unlike all other KIRs, KIR2DL4 has both
activating and inhibitory signaling domains. Here, we determined the 2.8 Å
crystal structure of the extracellular domains of KIR2DL4. Structurally, KIR2DL4
is reminiscent of other KIR2DL receptors, with the D0 and D2 adopting the
C2-type immunoglobulin fold arranged with an acute elbow angle. However, KIR2DL4
self-associated via the D0 domain in a concentration-dependent manner and was
observed as a tetramer in the crystal lattice by size exclusion chromatography,
dynamic light scattering, analytical ultracentrifugation, and small angle x-ray
scattering experiments. The assignment of residues in the D0 domain to forming
the KIR2DL4 tetramer precludes an interaction with HLA akin to that observed for
KIR3DL1. Accordingly, no interaction was observed to HLA by direct binding
studies. Our data suggest that the unique functional properties of KIR2DL4 may
be mediated by self-association of the receptor.
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Links
