Rationally designed mutations convert complexes of human recombinant T cell receptor ligands into monomers that retain biological activity

Journal of Chemical Technology and Biotechnology

Volumn 80, Issue 1, 2005, Pages 2-12

  Huan, Jianya Y ^a   Meza Romero, Roberto ^a   Mooney, Jeffery L ^a   Chou, Yuan K ^a   Edwards, David M ^a   Rich, Cathleen ^b   Link, Jason M ^b   Vandenbark, Arthur A ^a,b,c   Bourdette, Dennis N ^a   Bächinger, Hans Peter ^d   Burrows, Gregory G ^a,c  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b PORTLAND VA MEDICAL CENTER   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^d SHRINERS HOSPITAL FOR CHILDREN   (United States)

Author keywords

Autoimmunity; Drug design; Major histocompatibility complex; Protein structure

Indexed keywords

ANTIGENIC PEPTIDES; DYNAMIC LIGHT SCATTERING (DLS); MUTATIONS; T CELL RECEPTOR LIGANDS;

AGGLOMERATION; ANTIGENS; CHEMICAL MODIFICATION; ESCHERICHIA COLI; HYDROPHOBICITY; LIGHT SCATTERING; MONOMERS; MUTAGENESIS; SIZE EXCLUSION CHROMATOGRAPHY;

CELLS;

ASPARTIC ACID; HLA DR ANTIGEN; HLA DR2 ANTIGEN; HLA DR2B ANTIGEN; HLA DRA ANTIGEN; IMMUNOGLOBULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MONOMER; RECOMBINANT PROTEIN; SERINE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

BIOTECHNOLOGY;

ALLERGIC ENCEPHALOMYELITIS; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN SPECIFICITY; ARTICLE; BETA SHEET; BIOTINYLATION; CIRCULAR DICHROISM; COMPLEX FORMATION; CONTROLLED STUDY; COVALENT BOND; DRUG ACTIVITY; DRUG DESIGN; ESCHERICHIA COLI; FEMALE; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; LIGHT SCATTERING; LYMPHOCYTE PROLIFERATION; MALE; MOLECULAR RECOGNITION; MOUSE; MUTATIONAL ANALYSIS; NONHUMAN; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; QUANTITATIVE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; T LYMPHOCYTE;

ESCHERICHIA COLI;

EID: 19944429233     PISSN: 02682575     EISSN: None     Source Type: Journal    
DOI: 10.1002/jctb.1086     Document Type: Article

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