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Crystal structure of human immunoglobulin fragment Fab new refined at 2.0 Å esolution
Author(s) -
Saul Frederick A.,
Poljak Roberto J.
Publication year - 1992
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340140305
Subject(s) - complementarity determining region , crystallography , crystal structure , immunoglobulin light chain , fragment (logic) , chemistry , amino acid , resolution (logic) , immunoglobulin fab fragments , folding (dsp implementation) , physics , antibody , mathematics , biology , algorithm , computer science , biochemistry , engineering , electrical engineering , artificial intelligence , immunology
The three‐dimensional structure of the human immunoglobulin fragment Fab New (IgG1,λ) has been refined to a crystal‐lographic R ‐factor of 16.9% to 2Å resolution. Rms deviations of the final model from ideal geometry are 0.014 Å for bond distances and 3.03° for bond angles. Refinement was based on a new X‐ray data set including 28,301 reflections with F >2.5σ( F ) from 6.0 to 2.0 Å resolution. The starting model for the refinement procedure reported here is from the Brookhaven Protein Data Bank entry 3FAB (rev. 1981). Differences between the initial and final models include modified polypeptide‐chain folding in the third complementarity‐determining region (CDR3) and the third framework region (FR3) of V H and in some exposed loops of C L and C H l. Amino acid sequencechanges were determined at a number of positions by inspection of difference electron density maps. The incorporation of amino acid sequence changes results inan improved V H framework model for the “humanization” of monoclonal antibodies.