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Application of 13 C NMR spectroscopy to paratope mapping for larger antigen‐Fab complexes
Author(s) -
HaHyung Kim,
Koichi Kato,
Sumie Yamato,
Takako Igarashi,
Chigusa Matsunaga,
Hiroshi Ohtsuka,
Atsuko Higuchi,
Noriko Nomura,
Hiroshi Noguchi,
Yoshiaki Arata
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00486-2
Subject(s) - hapten , chemistry , paratope , antigen , nuclear magnetic resonance spectroscopy , molecule , stereochemistry , small molecule , biochemistry , microbiology and biotechnology , epitope , biology , genetics , organic chemistry
For the purpose of engineering the antibody combining site, mapping residues that are involved in antigen binding provide us with valuable information. By use of 13 C NMR spectroscopy with selectively 13 C‐labeled Fv fragments, we have established a general strategy to identify the residues that are perturbed upon binding of small antigen (hapten) molecules [(1990) Biochemistry 30, 6604–6610]. In the present paper, we demonstrate that this strategy can be extended to molecular structural analyses of the complexes of an Fab fragment and a larger antigen molecule such as Pseudomonas aeruginosa exotoxin A with a molecular mass of 67 kDa.