Document Detail

Peptides shorter than a minimal CTL epitope may have a higher binding affinity than the epitope for the class I Kk molecule.
MedLine Citation:
PMID:  7687804     Owner:  NLM     Status:  MEDLINE    
A previously published Kk-specific motif was used to predict that an optimal Kk-restricted epitope within the nucleoprotein (NP) of influenza A/PR/8/34 virus corresponds to sequence SDYEGRLI (residues 50-57). Although this is the minimal epitope recognized by murine cytotoxic T lymphocytes (CTL), its binding affinity for the Kk molecule is increased following removal of either the N-terminal amino acid residue (S) or the N-terminal dipeptide (SD). A possible explanation for this unexpected result is that interactions between the C-terminus of the epitope and the Kk molecule contribute to the binding energy to a much greater extent than interactions between the N-terminus of the epitope and the Kk molecule.
J Cossins; K Gould; G G Brownlee
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Virology     Volume:  195     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  1993 Aug 
Date Detail:
Created Date:  1993-08-20     Completed Date:  1993-08-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  851-4     Citation Subset:  IM    
Sir William Dunn School of Pathology, University of Oxford, United Kingdom.
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MeSH Terms
Amino Acid Sequence
Cell Line
H-2 Antigens / immunology*
Influenza A virus / immunology*
Molecular Sequence Data
Peptides / chemical synthesis,  immunology
T-Lymphocytes, Cytotoxic / immunology*
Reg. No./Substance:
0/Epitopes; 0/H-2 Antigens; 0/H-2K(K) antigen; 0/Peptides

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