Structure and humanization of a rat monoclonal Fab to human interleukin-5 | Zendy

William J. Cook | Zendy; Leigh J. Walter | Zendy; Nicholas Murgolo | Zendy; Chuan-Chu Chou | Zendy; Mary Petro | Zendy; Paul J. Zavodny | Zendy; Satwant K. Narula | Zendy; Lata Ramanathan | Zendy; Paul P. Trotta | Zendy; Tattanahalli L. Nagabhushan | Zendy

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Structure and humanization of a rat monoclonal Fab to human interleukin-5

Author(s) -

William J. Cook,

Leigh J. Walter,

Nicholas Murgolo,

Chuan-Chu Chou,

Mary Petro,

Paul J. Zavodny,

Satwant K. Narula,

Lata Ramanathan,

Paul P. Trotta,

Tattanahalli L. Nagabhushan

Publication year - 1996

Publication title -

protein engineering design and selection

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.627

H-Index - 109

eISSN - 1741-0134

pISSN - 1741-0126

DOI - 10.1093/protein/9.7.623

Subject(s) - monoclonal antibody , monoclonal , chemistry , microbiology and biotechnology , computational biology , biology , immunology , antibody

The X-ray crystal structure of a rat monoclonal Fab JES1-39D10, raised against recombinant human interleukin-5, has been determined with the use of molecular replacement techniques and refined at 2.7 A resolution by simulated annealing. The overall structure is similar to a murine Fab HyHEL-10 that is specific for hen egg white lysozyme. An interesting feature of the structure is the presence of leucine residues to support the H1 complementarity-determining region (CDR) loop. To our knowledge this is the first Fab crystal structure containing this unusual H1 loop support pattern. The activity of three humanized versions of 39D10 is explained by analysis of Fv interface residues and H1 support patterns of 39D10 and the human template HIL.

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