Cis-trans isomerization of the Epstein-Barr virus determinant peptide EENLLDFVRF after the DM1 TCR recognition of the HLA-B*4405/peptide complex (Journal article)

Stavrakoudis, A.

The Epstein-Barr virus determinant peptide EENLLDFVRF shows high immunogenicity when presented by HLA-B*4405 allotype. This fact is accompanied by a cis-trans isomerization of the Leu5-Asp6 peptide bond upon TCR binding of the pMHC complex. Molecular dynamics simulations of pMHC/TCR structures, with the EENLLDFVRF peptide in cis and trans conformations have been employed in order to examine the structure and dynamics of the pMHC complex with such an unusual conformation. The results, based on MM-PBSA free energy computations as well as buried surface area analysis and interactions at the pMHC/TCR interface, indicate that the TCR binds preferably the pMHC complex with the Leu5-Asp6 peptide bond in cis conformation. It is the first time that this notable conformational feature of T-cell epitope is investigated. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Οικονομικών και Κοινωνικών Επιστημών. Τμήμα Οικονομικών Επιστημών
Keywords: cis-trans peptide isomerization,class i mhc,epstein-barr virus nuclear antigen,hla-b44,molecular dynamics,peptide/mhc/tcr interactions,molecular-dynamics simulations,standard-deviation,poisson-boltzmann,free-energies,binding,conformation,proteins,electrostatics,flexibility,integration
URI: https://olympias.lib.uoi.gr/jspui/handle/123456789/11249
ISSN: 0014-5793
Link: <Go to ISI>://000286657700007
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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