Structural basis of MHC class I recognition by natural killer cell receptors.

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TitleStructural basis of MHC class I recognition by natural killer cell receptors.
Publication TypeJournal Article
Year of Publication2001
AuthorsSawicki, MW, Dimasi, N, Natarajan, K, Wang, J, Margulies, DH, Mariuzza, RA
JournalImmunol Rev
Date Published2001 Jun
KeywordsAmino Acid Sequence, Animals, Antigens, CD, Antigens, Ly, Binding Sites, Carrier Proteins, H-2 Antigens, Histocompatibility Antigens Class I, HLA-C Antigens, Humans, Killer Cells, Natural, Lectins, C-Type, Ligands, Macromolecular Substances, Membrane Proteins, Mice, Models, Molecular, Molecular Sequence Data, Molecular Structure, NK Cell Lectin-Like Receptor Subfamily A, Receptors, Immunologic, Receptors, KIR, Receptors, KIR2DL2, Receptors, NK Cell Lectin-Like, Sequence Homology, Amino Acid

Natural killer (NK)-cell function is regulated by NK receptors that recognize MHC class I (MHC-I) molecules on target cells. Two structurally distinct families of NK receptors have been identified, the immunoglobulin-like family (killer cell immunoglobulin-like receptors (KIRs), leukocyte immunoglobulin-like receptors (LIRs)) and the C-type lectin-like family (Ly49, CD94/NKG2A, NKG2D, CD69). Recently, the three-dimensional structures of several NK receptors were determined, in free form or bound to MHC-I. These include those of unbound KIRs, NKG2D, CD69, LIR-1 and the CD94 subunit of the CD94/NKG2A heterodimer. Together, these structures define the basic molecular architecture of both the immunoglobulin-like and C-type lectin-like families of NK receptors. In addition, crystal structures have been reported for the complex between Ly49A and H-2Dd, and for KIR2DL2 bound to HLA-Cw3. The complex structures provide a framework for understanding MHC-I recognition by NK receptors from both families and reveal striking differences in the nature of this recognition, despite the receptors' functional similarity.

Alternate JournalImmunol. Rev.
PubMed ID11513152
Grant ListR01 AI47900 / AI / NIAID NIH HHS / United States
R37 36900 / / PHS HHS / United States