Structural comparison of allogeneic and syngeneic T cell receptor-peptide-major histocompatibility complex complexes: A buried alloreactive mutation subtly alters peptide presentation substantially increasing Vβ interactions

Journal of Experimental Medicine

Volumn 195, Issue 9, 2002, Pages 1175-1186

  Luz, John G ^a   Huang, Mingdong ^a   Christopher Garcia, K ^a   Rudolph, Markus G ^a   Apostolopoulos, Vasso ^a   Teyton, Luc ^a   Wilson, Ian A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

T cell receptor; Alloreactivity; Antigen; Complementarity determining regions; TCR MHC recognition

Indexed keywords

ANTIGEN; ASPARTIC ACID; PEPTIDE; SERINE; T LYMPHOCYTE RECEPTOR;

ALLOIMMUNITY; ALPHA HELIX; ARTICLE; COMPARATIVE STUDY; COMPLEMENTARITY DETERMINING REGION; COMPLEX FORMATION; CRYSTAL STRUCTURE; GENE MUTATION; HYDROGEN BOND; MAJOR HISTOCOMPATIBILITY COMPLEX; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN STABILITY; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; H-2 ANTIGENS; HISTOCOMPATIBILITY ANTIGENS CLASS I; ISOANTIGENS; MAJOR HISTOCOMPATIBILITY COMPLEX; MODELS, MOLECULAR; MUTAGENESIS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RECEPTORS, ANTIGEN, T-CELL;

EID: 0037029674     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.20011644     Document Type: Article

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