Distinct conformations of Ly49 natural killer cell receptors mediate MHC class I recognition in trans and cis.

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Version: author
Serval ID
serval:BIB_4B901DC34A80
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Distinct conformations of Ly49 natural killer cell receptors mediate MHC class I recognition in trans and cis.
Journal
Immunity
Author(s)
Back J., Malchiodi E.L., Cho S., Scarpellino L., Schneider P., Kerzic M.C., Mariuzza R.A., Held W.
ISSN
1097-4180[electronic]
Publication state
Published
Issued date
2009
Peer-reviewed
Oui
Volume
31
Number
4
Pages
598-608
Language
english
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't Publication Status: ppublish
Abstract
Certain cell-surface receptors engage ligands expressed on juxtaposed cells and ligands on the same cell. The structural basis for trans versus cis binding is not known. Here, we showed that Ly49 natural killer (NK) cell receptors bound two MHC class I (MHC-I) molecules in trans when the two ligand-binding domains were backfolded onto the long stalk region. In contrast, dissociation of the ligand-binding domains from the stalk and their reorientation relative to the NK cell membrane allowed monovalent binding of MHC-I in cis. The distinct conformations (backfolded and extended) define the structural basis for cis-trans binding by Ly49 receptors and explain the divergent functional consequences of cis versus trans interactions. Further analyses identified specific stalk segments that were not required for MHC-I binding in trans but were essential for inhibitory receptor function. These data identify multiple distinct roles of stalk regions for receptor function.
Keywords
Animals, Histocompatibility Antigens Class I/immunology, Histocompatibility Antigens Class I/metabolism, Immunological Synapses/immunology, Immunological Synapses/metabolism, Killer Cells, Natural/immunology, Killer Cells, Natural/metabolism, Mice, Mice, Inbred C3H, NK Cell Lectin-Like Receptor Subfamily A/chemistry, NK Cell Lectin-Like Receptor Subfamily A/immunology, Protein Binding/immunology, Protein Conformation, Protein Multimerization
Pubmed
Web of science
Open Access
Yes
Create date
11/11/2009 12:48
Last modification date
20/08/2019 13:59
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