THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL

THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL

The adaptive immune response begins when CD4+ T cells recognize antigenic peptides bound to class II molecules of the Major Histocompatibility Complex (MHCII). The interaction between peptides and MHCII has been historically interpreted as a rigid docking event. However, this model has been challeng...

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Main Author: Andrea eFerrante
Format: Article
Language:English
Published: Frontiers Media S.A. 2013-10-01
Series:Frontiers in Immunology
Subjects:
Antigen Presentation
Thermodynamics
MHC class II
HLA-DM
Peptide binding
Online Access:http://journal.frontiersin.org/Journal/10.3389/fimmu.2013.00308/full
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spelling doaj-2fe23da288534f4e9e1d26f362b27d6a2020-11-25T00:53:51ZengFrontiers Media S.A.Frontiers in Immunology1664-32242013-10-01410.3389/fimmu.2013.0030864015THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUALAndrea eFerrante0University of Alaska FairbanksThe adaptive immune response begins when CD4+ T cells recognize antigenic peptides bound to class II molecules of the Major Histocompatibility Complex (MHCII). The interaction between peptides and MHCII has been historically interpreted as a rigid docking event. However, this model has been challenged by the evidence that conformational flexibility plays an important role in peptide-MHCII complex formation. Thermodynamic analysis of the binding reaction suggests a model of complexation in which the physical-chemical nature of the peptide determines the variability in flexibility of the substates in the peptide-MHC conformational ensemble. This review discusses our understanding of the correlation between thermodynamics of peptide binding and structural features of the resulting complex as well as their impact on HLA-DM activity and on our ability to predict MHCII-restricted epitopes.http://journal.frontiersin.org/Journal/10.3389/fimmu.2013.00308/fullAntigen PresentationThermodynamicsMHC class IIHLA-DMPeptide binding
collection DOAJ
language English
format Article
sources DOAJ
author Andrea eFerrante
spellingShingle Andrea eFerrante
THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
Frontiers in Immunology
Antigen Presentation
Thermodynamics
MHC class II
HLA-DM
Peptide binding
author_facet Andrea eFerrante
author_sort Andrea eFerrante
title THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
title_short THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
title_full THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
title_fullStr THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
title_full_unstemmed THERMODYNAMICS OF PEPTIDE-MHC CLASS II INTERACTIONS: NOT ALL COMPLEXES ARE CREATED EQUAL
title_sort thermodynamics of peptide-mhc class ii interactions: not all complexes are created equal
publisher Frontiers Media S.A.
series Frontiers in Immunology
issn 1664-3224
publishDate 2013-10-01
description The adaptive immune response begins when CD4+ T cells recognize antigenic peptides bound to class II molecules of the Major Histocompatibility Complex (MHCII). The interaction between peptides and MHCII has been historically interpreted as a rigid docking event. However, this model has been challenged by the evidence that conformational flexibility plays an important role in peptide-MHCII complex formation. Thermodynamic analysis of the binding reaction suggests a model of complexation in which the physical-chemical nature of the peptide determines the variability in flexibility of the substates in the peptide-MHC conformational ensemble. This review discusses our understanding of the correlation between thermodynamics of peptide binding and structural features of the resulting complex as well as their impact on HLA-DM activity and on our ability to predict MHCII-restricted epitopes.
topic Antigen Presentation
Thermodynamics
MHC class II
HLA-DM
Peptide binding
url http://journal.frontiersin.org/Journal/10.3389/fimmu.2013.00308/full
work_keys_str_mv AT andreaeferrante thermodynamicsofpeptidemhcclassiiinteractionsnotallcomplexesarecreatedequal
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