Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0086655
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dc.titleClustering HLA class I superfamilies using structural interaction patterns
dc.contributor.authorHarjanto S.
dc.contributor.authorNg L.F.P.
dc.contributor.authorTong J.C.
dc.date.accessioned2020-03-26T06:44:32Z
dc.date.available2020-03-26T06:44:32Z
dc.date.issued2014
dc.identifier.citationHarjanto S., Ng L.F.P., Tong J.C. (2014). Clustering HLA class I superfamilies using structural interaction patterns. PLoS ONE 9 (1) : e86655. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0086655
dc.identifier.issn19326203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/165962
dc.description.abstractHuman leukocyte antigen (HLA) class I molecules are critical components of the cell-mediated immune system that bind and present intracellular antigenic peptides to CD8+ T cell receptors. To understand the interaction mechanism underlying human leukocyte antigen (HLA) class I specificity in detail, we studied the structural interaction characteristics of 16,393 nonameric peptides binding to 58 HLA-A and -B molecules. Our analysis showed for the first time that HLA-peptide intermolecular bonding patterns vary among different alleles and may be grouped in a superfamily dependent manner. Through the use of these HLA class I 'fingerprints', a high resolution HLA class I superfamily classification schema was developed. This classification is capable of separating HLA alleles into well resolved, non-overlapping clusters, which is consistent with known HLA superfamily definitions. Such structural interaction approach serves as an excellent alternative to the traditional methods of HLA superfamily definitions that use peptide binding motifs or receptor information, and will help identify appropriate antigens suitable for broad-based subunit vaccine design. © 2014 Harjanto et al.
dc.publisherPublic Library of Science
dc.sourceUnpaywall 20200320
dc.subjectHLA A antigen
dc.subjectHLA B antigen
dc.subjectantibody combining site
dc.subjectantigen binding
dc.subjectarticle
dc.subjectgene cluster
dc.subjectgene frequency
dc.subjectgenetic variability
dc.subjectmolecular interaction
dc.subjectpeptide analysis
dc.subjectprocess development
dc.subjectstructure analysis
dc.subjectAmino Acid Sequence
dc.subjectCluster Analysis
dc.subjectComputational Biology
dc.subjectEpitopes, T-Lymphocyte
dc.subjectHLA-A Antigens
dc.subjectHLA-B Antigens
dc.subjectHumans
dc.subjectMolecular Sequence Data
dc.subjectMultigene Family
dc.subjectPeptides
dc.subjectProtein Binding
dc.typeArticle
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.1371/journal.pone.0086655
dc.description.sourcetitlePLoS ONE
dc.description.volume9
dc.description.issue1
dc.description.pagee86655
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