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Conserved structural features between HLA-DO beta and -DR beta.

J Thibodeau·P M Lavoie·A Samaan·J P Corre·R P Sékaly·P A Cazenave
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Abstract

HLA-DO is a non-classical MHC class II molecule presumed to play a specialized role in the antigen processing pathway. We have modeled the HLA-DO beta-chain and found its overall structure compatible with the one of DR beta. Functional studies further highlighted the similarity between these beta-chains of the class II family of proteins. Indeed, a mixed heterodimer composed of the DR alpha and a chimeric DO beta-chains presented bacterial superantigens to T cells and was shown to interact with CD4. The implications of such structural conservation for the in vivo functions of HLA-DO are discussed.

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Amino Acid SequenceAnimalsAntibodies, MonoclonalAntigen PresentationCell LineConserved SequenceDimerizationHLA-D AntigensHLA-DR AntigensHistocompatibility Antigens Class IIHumansHybridomasMiceModels, MolecularMolecular Sequence DataProtein ConformationProtein FoldingRecombinant Fusion ProteinsSequence Homology, Amino AcidT-LymphocytesTransfectionComparative StudyJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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J Thibodeau, P M Lavoie, A Samaan, J P Corre, R P Sékaly, P A Cazenave. 1998. Conserved structural features between HLA-DO beta and -DR beta.. https://doi.org/10.1016/s0161-5890(98)00061-3

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