Flexibility of the MHC class II peptide binding cleft in the bound, partially filled, and empty states: A molecular dynamics simulation study
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference59 articles.
1. The Biochemistry and Cell Biology of Antigen Processing and Presentation
2. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
3. Binding interactions between peptides and proteins of the class II Major Histocompatibility Complex
4. Structures of an MHC Class II Molecule with Covalently Bound Single Peptides
5. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides.
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2. Molecular mechanism of Be2+-ion binding to HLA-DP2: tetrahedral coordination, conformational changes and multi-ion binding;Physical Chemistry Chemical Physics;2020
3. HLA-DM Stabilizes the Empty MHCII Binding Groove: A Model Using Customized Natural Move Monte Carlo;Journal of Chemical Information and Modeling;2019-05-09
4. Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility;Frontiers in Immunology;2019-05-03
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