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- W2744957082 abstract "Structural biology of peptides presented by class I and class II MHC proteins has transformed immunology, impacting our understanding of fundamental immune mechanisms and allowing researchers to rationalize immunogenicity and design novel vaccines. However, proteins are not static structures as often inferred from crystallographic structures. Their components move and breathe individually and collectively over a range of timescales. Peptides bound within MHC peptide-binding grooves are no exception and their motions have been shown to impact recognition by T cell and other receptors in ways that influence function. Furthermore, peptides tune the motions of MHC proteins themselves, which impacts recognition of peptide/MHC complexes by other proteins. Here, we review the motional properties of peptides in MHC binding grooves and discuss how peptide properties can influence MHC motions. We briefly review theoretical concepts about protein motion and highlight key data that illustrate immunological consequences. We focus primarily on class I systems due to greater availability of data, but segue into class II systems as the concepts and consequences overlap. We suggest that characterization of the dynamic energy landscapes of peptide/MHC complexes and the resulting functional consequences is one of the next frontiers in structural immunology." @default.
- W2744957082 created "2017-08-17" @default.
- W2744957082 creator A5077419243 @default.
- W2744957082 creator A5079168905 @default.
- W2744957082 creator A5082462618 @default.
- W2744957082 date "2017-08-07" @default.
- W2744957082 modified "2023-10-16" @default.
- W2744957082 title "Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings" @default.
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- W2744957082 doi "https://doi.org/10.3389/fimmu.2017.00935" @default.
- W2744957082 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5545744" @default.
- W2744957082 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28824655" @default.
- W2744957082 hasPublicationYear "2017" @default.
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