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Volumn 54, Issue 5, 2000, Pages 318-327
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Changes at the floor of the peptide-binding groove induce a strong preference for proline at position 3 of the bound peptide: Molecular dynamics simulations of HLA-A*0217
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Author keywords
Class I major histocompatibility complex molecule; HLA A2 complex peptide binding motif; Secondary anchor residue
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Indexed keywords
ANTIGENS;
BIOCOMPATIBILITY;
CHEMICAL BONDS;
COMPOSITION EFFECTS;
COMPUTER SIMULATION;
IMMUNOLOGY;
MOLECULAR DYNAMICS;
MOLECULAR STRUCTURE;
TOXICITY;
MAJOR HISTOCOMPATIBILITY COMPLEX (MHC);
PEPTIDE;
AMINO ACIDS;
HLA A ANTIGEN;
MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING SITE;
COMPLEX FORMATION;
COMPUTER SIMULATION;
MOLECULAR DYNAMICS;
MOLECULAR INTERACTION;
PROTEIN PROTEIN INTERACTION;
STRUCTURE ACTIVITY RELATION;
AMINO ACID MOTIFS;
AMINO ACID SUBSTITUTION;
BINDING SITES;
COMPARATIVE STUDY;
COMPUTER SIMULATION;
HLA-A ANTIGENS;
HUMAN;
MODELS, MOLECULAR;
NONLINEAR DYNAMICS;
PEPTIDES;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
SUPPORT, NON-U.S. GOV'T;
TIME FACTORS;
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EID: 0034668132
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/1097-0282(20001015)54:5<318::AID-BIP30>3.0.CO;2-T Document Type: Article |
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Times cited : (17)
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References (39)
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