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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-12-28
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pubmed:databankReference |
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pubmed:abstractText |
NKG2D is known to trigger the natural killer (NK) cell lysis of various tumor and virally infected cells. In the NKG2D/ULBP3 complex, the structure of ULBP3 resembles the alpha1 and alpha2 domains of classical MHC molecules without a bound peptide. The lack of alpha3 and beta2m domains is compensated by replacing two hydrophobic patches at the underside of the class I MHC-like beta sheet floor with a group of hydrophilic and charged residues in ULBP3. NKG2D binds diagonally across the ULBP3 alpha helices, creating a complementary interface, an asymmetrical subunit orientation, and local conformational adjustments in the receptor. The interface is stabilized primarily by hydrogen bonds and hydrophobic interactions. Unlike the KIR receptors that recognize a conserved HLA region by a lock-and-key mechanism, NKG2D recognizes diverse ligands by an induced-fit mechanism.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fc receptor, neonatal,
http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HFE protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HLA Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-C*03 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-C Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/KLRK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/MHC class I-related chain A,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NK Cell Lectin-Like Receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/NK Cell Lectin-Like Receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Natural Killer Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ULBP3 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1074-7613
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1039-49
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11754823-Amino Acid Sequence,
pubmed-meshheading:11754823-Antigens, CD,
pubmed-meshheading:11754823-Carrier Proteins,
pubmed-meshheading:11754823-Crystallization,
pubmed-meshheading:11754823-Crystallography, X-Ray,
pubmed-meshheading:11754823-GPI-Linked Proteins,
pubmed-meshheading:11754823-HLA Antigens,
pubmed-meshheading:11754823-HLA-C Antigens,
pubmed-meshheading:11754823-Histocompatibility Antigens Class I,
pubmed-meshheading:11754823-Humans,
pubmed-meshheading:11754823-Hydrogen Bonding,
pubmed-meshheading:11754823-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:11754823-Killer Cells, Natural,
pubmed-meshheading:11754823-Lectins, C-Type,
pubmed-meshheading:11754823-Ligands,
pubmed-meshheading:11754823-Macromolecular Substances,
pubmed-meshheading:11754823-Membrane Glycoproteins,
pubmed-meshheading:11754823-Membrane Proteins,
pubmed-meshheading:11754823-Models, Molecular,
pubmed-meshheading:11754823-Molecular Sequence Data,
pubmed-meshheading:11754823-Multigene Family,
pubmed-meshheading:11754823-NK Cell Lectin-Like Receptor Subfamily D,
pubmed-meshheading:11754823-NK Cell Lectin-Like Receptor Subfamily K,
pubmed-meshheading:11754823-Protein Binding,
pubmed-meshheading:11754823-Protein Conformation,
pubmed-meshheading:11754823-Protein Structure, Tertiary,
pubmed-meshheading:11754823-Receptors, Antigen, T-Cell, alpha-beta,
pubmed-meshheading:11754823-Receptors, Fc,
pubmed-meshheading:11754823-Receptors, Immunologic,
pubmed-meshheading:11754823-Receptors, Natural Killer Cell,
pubmed-meshheading:11754823-Recombinant Fusion Proteins,
pubmed-meshheading:11754823-Sequence Alignment,
pubmed-meshheading:11754823-Sequence Homology, Amino Acid,
pubmed-meshheading:11754823-Structure-Activity Relationship
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pubmed:year |
2001
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pubmed:articleTitle |
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3.
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pubmed:affiliation |
Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 12441 Parklawn Drive, Rockville, MD 20852, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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