An antibody loop replacement design feasibility study and a loop-swapped dimer structure

Protein Engineering, Design and Selection

Volumn 22, Issue 2, 2009, Pages 93-101

  Clark, Louis A ^a,b   Boriack Sjodin, P Ann ^a   Day, Eric ^a   Eldredge, John ^a   Fitch, Christopher ^a   Jarpe, Matt ^a   Miller, Stephan ^a   Li, You ^a   Simon, Ken ^a   Van Vlijmen, Herman W T ^a  

^a BIOGEN   (United States)

^b R and D Project Development and Management   (United States)

Author keywords

Antibody loop design; Antibody structure; Binding affinity; Protein design; Protein stability

Indexed keywords

ANTIBODY STRUCTURE; ANTIBODY-ANTIGEN INTERFACES; BINDING AFFINITY; COMPLEMENTARITY-DETERMINING REGIONS; DESIGN APPROACHES; DESIGN FEASIBILITIES; DIMER STRUCTURES; DOMAIN SWAPPING; LENGTH-SCALE; LOGICAL TARGETS; LOOP RESIDUES; PROTEIN DESIGN; PROTEIN STABILITY; SIDE EFFECTS; STRUCTURAL INSTABILITIES; STRUCTURE-BASED; TRYPTOPHAN FLUORESCENCES;

AMINO ACIDS; BINDING ENERGY; CONFORMATIONS; CRYSTAL STRUCTURE; DESIGN; HYDROGEN; HYDROGEN BONDS; PLANNING; RESOURCE ALLOCATION; THERMAL EFFECTS;

ANTIBODIES;

ANTIBODY; COMPLEMENT; LEUCINE; MONOMER; SERINE; TRYPTOPHAN; VERY LATE ACTIVATION ANTIGEN 1;

AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ANTIBODY AFFINITY; ANTIBODY LOOP REPLACEMENT DESIGN; ANTIBODY STRUCTURE; ANTIGEN ANTIBODY REACTION; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; COMPLEMENTARITY DETERMINING REGION; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIMERIZATION; FEASIBILITY STUDY; FLUORESCENCE ANALYSIS; HYDROGEN BOND; LOOP SWAPPED DIMER STRUCTURE; MOLECULE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STABILITY;

ANIMALS; ANTIBODIES; ANTIBODY AFFINITY; CLONING, MOLECULAR; COMPLEMENTARITY DETERMINING REGIONS; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FEASIBILITY STUDIES; FLUORESCENCE; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; TEMPERATURE; TRYPTOPHAN;

EID: 61849182503     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn072     Document Type: Article

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