Dominance of an alternative CLIP sequence in the celiac disease associated HLA-DQ2 molecule
| dc.contributor.author | Wiesner, M. | en |
| dc.contributor.author | Stepniak, D. | en |
| dc.contributor.author | de Ru, A. H. | en |
| dc.contributor.author | Moustakis, A. K. | en |
| dc.contributor.author | Drijfhout, J. W. | en |
| dc.contributor.author | Papadopoulos, G. K. | en |
| dc.contributor.author | van Veelen, P. A. | en |
| dc.contributor.author | Koning, F. | en |
| dc.date.accessioned | 2015-11-24T19:23:47Z | |
| dc.date.available | 2015-11-24T19:23:47Z | |
| dc.identifier.issn | 0093-7711 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/22361 | |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Antigens, Differentiation, B-Lymphocyte/immunology/metabolism | en |
| dc.subject | Celiac Disease/*immunology | en |
| dc.subject | HLA-DQ Antigens/chemistry/genetics/*immunology | en |
| dc.subject | Histocompatibility Antigens Class II/immunology/metabolism | en |
| dc.subject | Humans | en |
| dc.subject | Mass Spectrometry | en |
| dc.subject | Models, Molecular | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Peptides/immunology/metabolism | en |
| dc.subject | Protein Binding | en |
| dc.subject | Protein Conformation | en |
| dc.title | Dominance of an alternative CLIP sequence in the celiac disease associated HLA-DQ2 molecule | en |
| heal.abstract | During assembly, HLA class II molecules associate with the invariant chain. As the result, the peptide-binding groove is occupied by an invariant chain peptide termed CLIP (class-II-associated invariant chain peptide; sequence MRMATPLLM). By mass spectrometry, we have now characterized peptides that are naturally present in HLA-DQ2. This analysis revealed that 22 variants of Ii-derived peptides are associated with HLA-DQ2. Strikingly, the large majority of those do not contain the conventional CLIP sequence MRMATPLLM, but instead a peptide that partially overlaps with CLIP, sequence TPLLMQALPM. Peptide binding studies indicate that this alternative CLIP peptide has superior HLA-DQ2 binding properties compared to the conventional CLIP and that the minimal nine-amino-acid binding core consists of the sequence PLLMQALPM, findings that could be corroborated by molecular simulation. The alternative CLIP peptide was also found to be present in HLA-DQ2 molecules isolated from human thymus. Moreover, the alternative CLIP peptide was also found in association with HLA-DQ8. Together, these results indicate that HLA-DQ2 and HLA-DQ8 associate with an alternative CLIP sequence, a property that may relate to the strong association between HLA-DQ molecules and human autoimmune diseases. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | 10.1007/s00251-008-0310-6 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/18584168 | - |
| heal.identifier.secondary | http://www.springerlink.com/content/w2215071175l106v/fulltext.pdf | - |
| heal.journalName | Immunogenetics | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2008 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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