Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0198-8859(01)00219-1
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dc.titleTowards the MHC-peptide combinatorics
dc.contributor.authorKangueane, P.
dc.contributor.authorSakharkar, M.K.
dc.contributor.authorKolatkar, P.R.
dc.contributor.authorRen, E.C.
dc.date.accessioned2012-03-28T06:06:52Z
dc.date.available2012-03-28T06:06:52Z
dc.date.issued2001
dc.identifier.citationKangueane, P., Sakharkar, M.K., Kolatkar, P.R., Ren, E.C. (2001). Towards the MHC-peptide combinatorics. Human Immunology 62 (5) : 539-556. ScholarBank@NUS Repository. https://doi.org/10.1016/S0198-8859(01)00219-1
dc.identifier.issn01988859
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/31520
dc.description.abstractThe exponentially increased sequence information on major histocompatibility complex (MHC) alleles points to the existence of a high degree of polymorphism within them. To understand the functional consequences of MHC alleles, 36 nonredundant MHC-peptide complexes in the protein data bank (PDB) were examined. Induced fit molecular recognition patterns such as those in MHC-peptide complexes are governed by numerous rules. The 36 complexes were clustered into 19 subgroups based on allele specificity and peptide length. The subgroups were further analyzed for identifying common features in MHC-peptide binding pattern. The four major observations made during the investigation were: (1) the positional preference of peptide residues defined by percentage burial upon complex formation is shown for all the 19 subgroups and the burial profiles within entries in a given subgroup are found to be similar; (2) in class I specific 8- and 9-mer peptides, the fourth residue is consistently solvent exposed, however this observation is not consistent in class I specific 10-mer peptides; (3) an anchor-shift in positional preference is observed towards the C terminal as the peptide length increases in class II specific peptides; and (4) peptide backbone atoms are proportionately dominant at the MHC-peptide interface. © American Society for Histocompatibility and Immunogenetics, 2001. Published by Elsevier Science Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0198-8859(01)00219-1
dc.sourceScopus
dc.subjectBinding pattern
dc.subjectBinding value
dc.subjectMHC-peptide interface
dc.subjectResidue preference
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.contributor.departmentBIOINFORMATICS CENTRE
dc.contributor.departmentGENOME INSTITUTE OF SINGAPORE
dc.description.doi10.1016/S0198-8859(01)00219-1
dc.description.sourcetitleHuman Immunology
dc.description.volume62
dc.description.issue5
dc.description.page539-556
dc.description.codenHUIMD
dc.identifier.isiut000168550200011
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