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A HLA-DRB supertype chart with potential overlapping peptide binding function.

Mohanapriya A, Nandagond S, Shapshak P, Kangueane U, Kangueane P - Bioinformation (2010)

Bottom Line: HLA-DRB alleles are class II alleles that are associated with CD4+ T-cell immune response.Definition of DRB supertypes using binding data is limited to few (about 29) known alleles (< 5% of all known DRB alleles).Hence, we describe a strategy using structurally defined virtual pockets to group all known DRB alleles with regard to their overlapping peptide binding specificity.

View Article: PubMed Central - PubMed

Affiliation: Biomedical Informatics, Pondicherry 607 402, India; VITU, Vellore, Tamil Nadu 632 014, India.

ABSTRACT
HLA-DRB alleles are class II alleles that are associated with CD4+ T-cell immune response. DRB alleles are polymorphic and currently there are about 622 named in the IMGT/HLA sequence database. Each allele binds short peptides with high sensitivity and specificity. However, it has been suggested that majority of HLA alleles can be covered within few HLA supertypes, where different members of a supertype bind similar peptides showing distinct repertoires. Definition of DRB supertypes using binding data is limited to few (about 29) known alleles (< 5% of all known DRB alleles). Hence, we describe a strategy using structurally defined virtual pockets to group all known DRB alleles with regard to their overlapping peptide binding specificity.

No MeSH data available.


The peptide binding groove is formed by two domains each from alpha and beta chains
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Figure 2: The peptide binding groove is formed by two domains each from alpha and beta chains

Mentions: The peptide binding groove is formed by two domains each from alphaand beta chains (Figure 2). The β1 domain (first 90 residues in the Nterminal) from beta chain that constitutes the peptide binding groove isconsidered for further analysis.


A HLA-DRB supertype chart with potential overlapping peptide binding function.

Mohanapriya A, Nandagond S, Shapshak P, Kangueane U, Kangueane P - Bioinformation (2010)

The peptide binding groove is formed by two domains each from alpha and beta chains
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2957767&req=5

Figure 2: The peptide binding groove is formed by two domains each from alpha and beta chains
Mentions: The peptide binding groove is formed by two domains each from alphaand beta chains (Figure 2). The β1 domain (first 90 residues in the Nterminal) from beta chain that constitutes the peptide binding groove isconsidered for further analysis.

Bottom Line: HLA-DRB alleles are class II alleles that are associated with CD4+ T-cell immune response.Definition of DRB supertypes using binding data is limited to few (about 29) known alleles (< 5% of all known DRB alleles).Hence, we describe a strategy using structurally defined virtual pockets to group all known DRB alleles with regard to their overlapping peptide binding specificity.

View Article: PubMed Central - PubMed

Affiliation: Biomedical Informatics, Pondicherry 607 402, India; VITU, Vellore, Tamil Nadu 632 014, India.

ABSTRACT
HLA-DRB alleles are class II alleles that are associated with CD4+ T-cell immune response. DRB alleles are polymorphic and currently there are about 622 named in the IMGT/HLA sequence database. Each allele binds short peptides with high sensitivity and specificity. However, it has been suggested that majority of HLA alleles can be covered within few HLA supertypes, where different members of a supertype bind similar peptides showing distinct repertoires. Definition of DRB supertypes using binding data is limited to few (about 29) known alleles (< 5% of all known DRB alleles). Hence, we describe a strategy using structurally defined virtual pockets to group all known DRB alleles with regard to their overlapping peptide binding specificity.

No MeSH data available.