Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3
Author
Radaev, S; Rostro, B; Brooks, AG; Colonna, M; Sun, PDDate
2001-12-01Source Title
IMMUNITYPublisher
CELL PRESSUniversity of Melbourne Author/s
Brooks, AndrewAffiliation
Microbiology And ImmunologyMetadata
Show full item recordDocument Type
Journal ArticleCitations
Radaev, S., Rostro, B., Brooks, A. G., Colonna, M. & Sun, P. D. (2001). Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3. IMMUNITY, 15 (6), pp.1039-1049. https://doi.org/10.1016/S1074-7613(01)00241-2.Access Status
This item is currently not available from this repositoryDescription
C1 - Journal Articles Refereed
Abstract
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.
Keywords
Cellular Immunology; Immune System and AllergyExport Reference in RIS Format
Endnote
- Click on "Export Reference in RIS Format" and choose "open with... Endnote".
Refworks
- Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References