Please use this identifier to cite or link to this item:
https://scholarbank.nus.edu.sg/handle/10635/34643
DC Field | Value | |
---|---|---|
dc.title | CHARACTERISATION OF MHC-PEPTIDE BINDING SPECIFICITIES BY STRUCTURAL STUDIES | |
dc.contributor.author | TOH XINYU | |
dc.date.accessioned | 2012-09-12T18:00:13Z | |
dc.date.available | 2012-09-12T18:00:13Z | |
dc.date.issued | 2012-05-17 | |
dc.identifier.citation | TOH XINYU (2012-05-17). CHARACTERISATION OF MHC-PEPTIDE BINDING SPECIFICITIES BY STRUCTURAL STUDIES. ScholarBank@NUS Repository. | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/34643 | |
dc.description.abstract | The human leukocyte antigen (HLA)-C molecules have emerged to have a role in T-cell immunity apart from its dominant role in NK cell recognition. Molecular and structural characterisation of HLA-C molecules has been impeded by its low surface expression and poor assembly. Therefore, a set of refined folding and purification scheme have been developed for HLA-C structural determination. For the first time in 10 years, the crystal structures of 2 novel HLA-C molecules coupled with viral peptides are presented. HLA-C*08:01 is not only able to bind the Cytomegalovirus pp65 peptide (VVCAHELVC) known to elicit a cytotoxic T-cell response but also bind the Influenza matrix peptide (GILGFVFTL) which is HLA-A*02-restricted. The structures, presented at a high resolution of 2.18Å and 1.84Å, allow the examination of HLA-C peptide binding specificities in greater detail and provide a structural basis of HLA-C-peptide complex formation to understand the unique role of HLA-C in immunity. | |
dc.language.iso | en | |
dc.subject | HLA-C | |
dc.type | Thesis | |
dc.contributor.department | MICROBIOLOGY | |
dc.contributor.supervisor | REN EE CHEE | |
dc.description.degree | Ph.D | |
dc.description.degreeconferred | DOCTOR OF PHILOSOPHY | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Ph.D Theses (Open) |
Show simple item record
Files in This Item:
File | Description | Size | Format | Access Settings | Version | |
---|---|---|---|---|---|---|
TohXY.pdf | 12.28 MB | Adobe PDF | OPEN | None | View/Download |
Google ScholarTM
Check
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.