DOI: 10.1016/0014-5793(93)80963-u. <sup>13</sup>C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G

13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G

10.1016/0014-5793(93)80963-u

Crossref journal-article

Wiley

FEBS Letters (311)

Abstract

The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy. Mouse IgG1, IgG2a, and IgG2b proteins have been selectively labeled with 13C at the carbonyl carbon of His, Met, Trp or Tyr residue and used to prepare the corresponding Fc fragments by limited proteolysis. Site‐specific resonance assignments have been made for each of these Fc analogues. FB was reported to form two contacts (contact 1 and contact 2) with human Fc in the crystal [Biochemistry 20 (1981) 2361‐2370]. Comparisons of the chemical shift data of the Fc fragments observed in the absence and presence of FB have led us to conclude that in solution contact 1 is responsible for the formation of the Fc‐FB complexes.

Bibliography

Kato, K., Gouda, H., Takaha, W., Yoshino, A., Matsunaga, C., & Arata, Y. (1993). 13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G. FEBS Letters, 328(1â2), 49â54. Portico.

Authors 6

Koichi Kato (first)
Hiroaki Gouda (additional)
Wakana Takaha (additional)
Atsuko Yoshino (additional)
Chigusa Matsunaga (additional)
Yoji Arata (additional)

References 25 Referenced 34

10.1016/S0065-2776(08)60722-1
10.1016/0161-5890(85)90151-8
10.1111/j.1432-1033.1986.tb09625.x
10.1021/bi00512a001
10.1021/bi00155a020
10.1016/0014-5793(75)80636-3
10.1042/bj1670661
10.1016/0006-291X(78)91206-8
10.1093/oxfordjournals.jbchem.a122769
Kato K. Matsunaga C. Igarashi T. Kim H. Odaka A. Shimada I. and Arata Y. (1991a) Biochemistry 30 270-278. (10.1021/bi00215a037)
Kato K. Matsunaga C. Odaka A. Yamato S. Takaha W. Shimada I. and Arata Y. (1991b) Biochemistry 30 6604-6610. (10.1021/bi00240a033)
10.1007/BF02192861
10.1016/0022-1759(92)90325-N
10.1111/j.1432-1033.1981.tb06299.x
10.1093/protein/2.6.481
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10.1002/cyto.990020607
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10.1002/prot.340020203
10.1073/pnas.63.1.78
{'key': 'e_1_2_1_25_1', 'volume-title': 'Sequences of Proteins of Immunological Interrest', 'author': 'Kabat E.A.', 'year': '1987'} / Sequences of Proteins of Immunological Interrest by Kabat E.A. (1987)
10.1021/bi00476a013

Dates

Type	When
Created	23 years, 1 month ago (July 25, 2002, 3:41 a.m.)
Deposited	1 year, 11 months ago (Sept. 16, 2023, 12:19 a.m.)
Indexed	1 year, 2 months ago (June 23, 2024, 12:35 a.m.)
Issued	32 years ago (Aug. 9, 1993)
Published	32 years ago (Aug. 9, 1993)
Published Online	23 years, 9 months ago (Nov. 12, 2001)
Published Print	32 years ago (Aug. 9, 1993)

Funders 0

None

BibTeX

@article{Kato_1993, title={13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G}, volume={328}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(93)80963-u}, DOI={10.1016/0014-5793(93)80963-u}, number={1–2}, journal={FEBS Letters}, publisher={Wiley}, author={Kato, Koichi and Gouda, Hiroaki and Takaha, Wakana and Yoshino, Atsuko and Matsunaga, Chigusa and Arata, Yoji}, year={1993}, month=aug, pages={49–54} }

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