Crystal structures of two I-A(d)-peptide complexes reveal that high affinity can be achieved without large anchor residues

Immunity

Volumn 8, Issue 3, 1998, Pages 319-329

  Scott, C A ^a   Peterson, P A ^b   Teyton, L ^a   Wilson, I A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b JOHNSON AND JOHNSON PHARMACEUTICAL RESEARCH AND DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; OVALBUMIN; PEPTIDE; T LYMPHOCYTE RECEPTOR; VIRUS HEMAGGLUTININ;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; AUTOIMMUNE DISEASE; BINDING AFFINITY; COMPLEX FORMATION; CRYSTAL STRUCTURE; INFLUENZA VIRUS; INSULIN DEPENDENT DIABETES MELLITUS; MAJOR HISTOCOMPATIBILITY COMPLEX; MOUSE; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; RHEUMATOID ARTHRITIS; T LYMPHOCYTE ACTIVATION; X RAY CRYSTALLOGRAPHY;

EID: 0032033678     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80537-3     Document Type: Article

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