We are analyzing https://link.springer.com/article/10.1007/s002510050162.

Title:
A roadmap for HLA-A, HLA-B, and HLA-C peptide binding specificities | Immunogenetics
Description:
The high level of polymorphism in major histocompatibility complex (MHC) molecules leads to many allele-specific peptide binding repertoires that can generally be characterized by sequence motifs. Such motifs have previously been elucidated experimentally for several MHC molecules and shown to bind in specificity pockets in the antigen binding cleft. Here, a new and less restrictive description of the traditional antigen binding pockets is derived. These regions are referred to as peptide binding environments and are defined as those residues in a fixed neighborhood of the peptide residues in known crystal structure complexes. By examining the antigen binding environments from MHC molecules with known motifs, we made predictions as to likely motifs for other MHC molecules which share the same environments. The predictions are presented in the form of Tables and are pertinent to class I HLA-A, HLA-B, and HLA-C MHC sequences, and are shown to correlate well with experiments.
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Keywords {🔍}

article, binding, peptide, mhc, access, privacy, cookies, content, motifs, information, publish, research, search, molecules, open, data, log, journal, immunogenetics, hlaa, hlab, hlac, chelvanayagam, antigen, environments, class, discover, springer, optional, personal, parties, policy, find, track, roadmap, specificities, cite, explore, major, histocompatibility, complex, sequence, shown, specificity, pockets, residues, complexes, predictions, institution, learning,

Topics {✒️}

major histocompatibility complex connecting mhc-i-binding motifs peptide binding specificities proteins mhc class month download article/chapter peptide binding environments antigen binding cleft antigen binding environments privacy choices/manage cookies full article pdf article immunogenetics aims specificity pockets crystal structure complexes sequence motifs european economic area scope submit manuscript check access john curtin school instant access conditions privacy policy accepting optional cookies peptide residues article chelvanayagam machine learning journal finder publish article log mhc molecules mhc sequences related subjects article cite privacy policy personal data books a optional cookies manage preferences derived class subscription content similar content data protection essential cookies cookies skip mhc institution subscribe journal publish information usage analysis social media varying standards november 1996 volume 45

Schema {🗺️}

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         description: The high level of polymorphism in major histocompatibility complex (MHC) molecules leads to many allele-specific peptide binding repertoires that can generally be characterized by sequence motifs. Such motifs have previously been elucidated experimentally for several MHC molecules and shown to bind in specificity pockets in the antigen binding cleft. Here, a new and less restrictive description of the traditional antigen binding pockets is derived. These regions are referred to as peptide binding environments and are defined as those residues in a fixed neighborhood of the peptide residues in known crystal structure complexes. By examining the antigen binding environments from MHC molecules with known motifs, we made predictions as to likely motifs for other MHC molecules which share the same environments. The predictions are presented in the form of Tables and are pertinent to class I HLA-A, HLA-B, and HLA-C MHC sequences, and are shown to correlate well with experiments.
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            Major Histocompatibility Complex
            Binding Specificity
            Binding Pocket
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            Immunology
            Human Genetics
            Gene Function
            Cell Biology
            Allergology
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      description: The high level of polymorphism in major histocompatibility complex (MHC) molecules leads to many allele-specific peptide binding repertoires that can generally be characterized by sequence motifs. Such motifs have previously been elucidated experimentally for several MHC molecules and shown to bind in specificity pockets in the antigen binding cleft. Here, a new and less restrictive description of the traditional antigen binding pockets is derived. These regions are referred to as peptide binding environments and are defined as those residues in a fixed neighborhood of the peptide residues in known crystal structure complexes. By examining the antigen binding environments from MHC molecules with known motifs, we made predictions as to likely motifs for other MHC molecules which share the same environments. The predictions are presented in the form of Tables and are pertinent to class I HLA-A, HLA-B, and HLA-C MHC sequences, and are shown to correlate well with experiments.
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         Human Genetics
         Gene Function
         Cell Biology
         Allergology
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