Please use this identifier to cite or link to this item:
|Title:||Compression of functional space in HLA-A sequence diversity|
|Citation:||Zhao, B., Sakharkar, M.K., Kangueane, P., Png, A.E.H., Ren, E.C., Kolatkar, P.R., Mathura, V.S. (2003). Compression of functional space in HLA-A sequence diversity. Human Immunology 64 (7) : 718-728. ScholarBank@NUS Repository. https://doi.org/10.1016/S0198-8859(03)00078-8|
|Abstract:||The major histocompatibility complex (MHC) is highly polymorphic and more than 1500 human MHC alleles are known to date. These alleles do not bind to a given peptide with identical affinity. Although MHC alleles are functionally related, it is difficult to quantify the functional variation between them. Three-dimensional structures of known MHC-peptide (MHCp) complexes suggest that specific peptide residues bind selectively to functional pockets in the binding groove. From a set of known MHCp structures we identified 21 critical polymorphic functional residue positions (CPFRP) that significantly reduced functional pocket variability to just 189 among 212 HLA-A alleles. Interestingly 101 HLA-A alleles clustered into 29 clusters such that the six functional pockets formed by the CPFRPs are identical within the cluster. © American Society for Histocompatibility and Immunogenetics, 2003. Published by Elsevier Inc.|
|Source Title:||Human Immunology|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jul 21, 2018
WEB OF SCIENCETM
checked on Jun 11, 2018
checked on Jul 13, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.