An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.
The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals th...
| Main Authors: | , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
1996
|
| _version_ | 1797095170047475712 |
|---|---|
| author | Smith, K Reid, S Stuart, D McMichael, A Jones, E Bell, J |
| author_facet | Smith, K Reid, S Stuart, D McMichael, A Jones, E Bell, J |
| author_sort | Smith, K |
| collection | OXFORD |
| description | The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix. |
| first_indexed | 2024-03-07T04:24:03Z |
| format | Journal article |
| id | oxford-uuid:cc03de49-e408-4914-be81-94447af0ff67 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:24:03Z |
| publishDate | 1996 |
| record_format | dspace |
| spelling | oxford-uuid:cc03de49-e408-4914-be81-94447af0ff672022-03-27T07:18:46ZAn altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cc03de49-e408-4914-be81-94447af0ff67EnglishSymplectic Elements at Oxford1996Smith, KReid, SStuart, DMcMichael, AJones, EBell, JThe crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix. |
| spellingShingle | Smith, K Reid, S Stuart, D McMichael, A Jones, E Bell, J An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title | An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title_full | An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title_fullStr | An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title_full_unstemmed | An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title_short | An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. |
| title_sort | altered position of the alpha 2 helix of mhc class i is revealed by the crystal structure of hla b 3501 |
| work_keys_str_mv | AT smithk analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT reids analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT stuartd analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT mcmichaela analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT jonese analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT bellj analteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT smithk alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT reids alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT stuartd alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT mcmichaela alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT jonese alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 AT bellj alteredpositionofthealpha2helixofmhcclassiisrevealedbythecrystalstructureofhlab3501 |