Coupling between side chain interactions and binding pocket flexibility in HLA-B*44:02 molecules investigated by molecular dynamics simulations

Molecular Immunology

Volumn 63, Issue 2, 2015, Pages 312-319

  Ostermeir, Katja ^a   Springer, Sebastian ^b   Zacharias, Martin ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b JACOBS UNIVERSITY BREMEN   (Germany)

Author keywords

Accelerated sampling; Free energy calculation; MHC class I molecule; Peptide editing, Molecular simulation; Peptide loading

Indexed keywords

ALLOANTIGEN; ARGININE; ASPARAGINE; ASPARTIC ACID; HLA B 44:02 ANTIGEN; HLA B 44:05 ANTIGEN; HLA B ANTIGEN; SODIUM CHLORIDE; TAPASIN; UNCLASSIFIED DRUG; AMINO ACID; HLA B44 ANTIGEN; PEPTIDE; PROTEIN BINDING;

ALLOSTERISM; AMINO ACID SEQUENCE; ANTIGEN ANTIBODY REACTION; ANTIGEN BINDING; ANTIGEN PRESENTATION; ANTIGEN STRUCTURE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GENE REARRANGEMENT; HUMAN; HYDROGEN BOND; MOLECULAR DYNAMICS; PROTEIN CONFORMATION; PROTEIN INTERACTION; BINDING SITE; CHEMISTRY; METABOLISM; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

AMINO ACIDS; BINDING SITES; HLA-B44 ANTIGEN; HUMANS; MOLECULAR DYNAMICS SIMULATION; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 84912045330     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2014.07.021     Document Type: Article

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