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PDBsum entry 5j6g
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Immune system
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PDB id
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5j6g
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Contents |
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272 a.a.
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99 a.a.
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122 a.a.
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PDB id:
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Immune system
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Title:
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Recognition of the mhc class ib molecule h2-q10 by the natural killer cell receptor ly49c
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Structure:
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H-2 class i histocompatibility antigen, q10 alpha chain. Chain: a, c. Engineered: yes. Beta-2-microglobulin. Chain: b, d. Engineered: yes. Val-gly-ile-thr-asn-val-asp-leu. Chain: e, f. Engineered: yes.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-q10. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b2m. Synthetic: yes. Gene: klra3, ly-49c, ly49c.
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Resolution:
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3.30Å
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R-factor:
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0.222
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R-free:
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0.253
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Authors:
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R.Berry,J.Rossjohn
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Key ref:
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L.C.Sullivan
et al.
(2016).
Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C.
J Biol Chem,
291,
18740-18752.
PubMed id:
DOI:
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Date:
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04-Apr-16
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Release date:
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13-Jul-16
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PROCHECK
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Headers
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References
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P01898
(HA10_MOUSE) -
H-2 class I histocompatibility antigen, Q10 alpha chain from Mus musculus
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Seq:
Struc:
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325 a.a.
272 a.a.
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DOI no:
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J Biol Chem
291:18740-18752
(2016)
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PubMed id:
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Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C.
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L.C.Sullivan,
R.Berry,
N.Sosnin,
J.M.Widjaja,
F.A.Deuss,
G.R.Balaji,
N.L.LaGruta,
M.Mirams,
J.A.Trapani,
J.Rossjohn,
A.G.Brooks,
D.M.Andrews.
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ABSTRACT
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Murine natural killer (NK) cells are regulated by the interaction of Ly49
receptors with major histocompatibility complex class I molecules (MHC-I).
Although the ligands for inhibitory Ly49 were considered to be restricted to
classical MHC (MHC-Ia), we have shown that the non-classical MHC molecule
(MHC-Ib) H2-M3 was a ligand for the inhibitory Ly49A. Here we establish that
another MHC-Ib, H2-Q10, is a bona fide ligand for the inhibitory Ly49C receptor.
H2-Q10 bound to Ly49C with a marginally lower affinity (∼5 μm) than that
observed between Ly49C and MHC-Ia (H-2K(b)/H-2D(d), both ∼1 μm), and this
recognition could be prevented by cis interactions with H-2K in situ To
understand the molecular details underpinning Ly49·MHC-Ib recognition, we
determined the crystal structures of H2-Q10 and Ly49C bound H2-Q10. Unliganded
H2-Q10 adopted a classical MHC-I fold and possessed a peptide-binding groove
that exhibited features similar to those found in MHC-Ia, explaining the diverse
peptide binding repertoire of H2-Q10. Ly49C bound to H2-Q10 underneath the
peptide binding platform to a region that encompassed residues from the α1,
α2, and α3 domains, as well as the associated β2-microglobulin subunit. This
docking mode was conserved with that previously observed for Ly49C·H-2K(b)
Indeed, structure-guided mutation of Ly49C indicated that Ly49C·H2-Q10 and
Ly49C·H-2K(b) possess similar energetic footprints focused around residues
located within the Ly49C β4-stand and L5 loop, which contact the underside of
the peptide-binding platform floor. Our data provide a structural basis for
Ly49·MHC-Ib recognition and demonstrate that MHC-Ib represent an extended
family of ligands for Ly49 molecules.
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Links
