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Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501

The human leukocyte antigen (HLA) class I system comprises a highly polymorphic set of molecules that specifically bind and present peptides to cytotoxic T cells. HLA-B*1501 is a prototypical member of the HLA-B62 supertype and only two peptide–HLA-B*1501 structures have been determined. Here, the c...

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Autores principales: Røder, Gustav, Kristensen, Ole, Kastrup, Jette S., Buus, Søren, Gajhede, Michael
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2496847/
https://www.ncbi.nlm.nih.gov/pubmed/18540051
http://dx.doi.org/10.1107/S1744309108012396
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author Røder, Gustav
Kristensen, Ole
Kastrup, Jette S.
Buus, Søren
Gajhede, Michael
author_facet Røder, Gustav
Kristensen, Ole
Kastrup, Jette S.
Buus, Søren
Gajhede, Michael
author_sort Røder, Gustav
collection PubMed
description The human leukocyte antigen (HLA) class I system comprises a highly polymorphic set of molecules that specifically bind and present peptides to cytotoxic T cells. HLA-B*1501 is a prototypical member of the HLA-B62 supertype and only two peptide–HLA-B*1501 structures have been determined. Here, the crystal structure of HLA-B*1501 in complex with a SARS coronavirus-derived nonapeptide (VQQESSFVM) has been determined at high resolution (1.87 Å). The peptide is deeply anchored in the B and F pockets, but with the Glu4 residue pointing away from the floor in the peptide-binding groove, making it available for interactions with a potential T-cell receptor.
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spelling pubmed-24968472009-06-01 Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501 Røder, Gustav Kristensen, Ole Kastrup, Jette S. Buus, Søren Gajhede, Michael Acta Crystallogr Sect F Struct Biol Cryst Commun Protein Structure Communications The human leukocyte antigen (HLA) class I system comprises a highly polymorphic set of molecules that specifically bind and present peptides to cytotoxic T cells. HLA-B*1501 is a prototypical member of the HLA-B62 supertype and only two peptide–HLA-B*1501 structures have been determined. Here, the crystal structure of HLA-B*1501 in complex with a SARS coronavirus-derived nonapeptide (VQQESSFVM) has been determined at high resolution (1.87 Å). The peptide is deeply anchored in the B and F pockets, but with the Glu4 residue pointing away from the floor in the peptide-binding groove, making it available for interactions with a potential T-cell receptor. International Union of Crystallography 2008-05-17 /pmc/articles/PMC2496847/ /pubmed/18540051 http://dx.doi.org/10.1107/S1744309108012396 Text en © International Union of Crystallography 2008
spellingShingle Protein Structure Communications
Røder, Gustav
Kristensen, Ole
Kastrup, Jette S.
Buus, Søren
Gajhede, Michael
Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title_full Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title_fullStr Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title_full_unstemmed Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title_short Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501
title_sort structure of a sars coronavirus-derived peptide bound to the human major histocompatibility complex class i molecule hla-b*1501
topic Protein Structure Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2496847/
https://www.ncbi.nlm.nih.gov/pubmed/18540051
http://dx.doi.org/10.1107/S1744309108012396
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