Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.
The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B p...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1996
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| _version_ | 1797089358735474688 |
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| author | Smith, K Reid, S Harlos, K McMichael, A Stuart, D Bell, J Jones, E |
| author_facet | Smith, K Reid, S Harlos, K McMichael, A Stuart, D Bell, J Jones, E |
| author_sort | Smith, K |
| collection | OXFORD |
| description | The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes. |
| first_indexed | 2024-03-07T03:03:00Z |
| format | Journal article |
| id | oxford-uuid:b193fcc8-7422-411d-a1bf-75f20473c050 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:03:00Z |
| publishDate | 1996 |
| record_format | dspace |
| spelling | oxford-uuid:b193fcc8-7422-411d-a1bf-75f20473c0502022-03-27T04:05:07ZBound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b193fcc8-7422-411d-a1bf-75f20473c050EnglishSymplectic Elements at Oxford1996Smith, KReid, SHarlos, KMcMichael, AStuart, DBell, JJones, EThe structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes. |
| spellingShingle | Smith, K Reid, S Harlos, K McMichael, A Stuart, D Bell, J Jones, E Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title | Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title_full | Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title_fullStr | Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title_full_unstemmed | Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title_short | Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. |
| title_sort | bound water structure and polymorphic amino acids act together to allow the binding of different peptides to mhc class i hla b53 |
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