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Title: Sequential sup 1 H NMR assignments and secondary structure of the B domain of staphylococcal protein A: Structural changes between the free B domain in solution and the Fc-bound B domain in crystal

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00489a040· OSTI ID:5920959
; ;  [1]; ;  [2]
  1. Univ. of Tokyo (Japan)
  2. Kyowa Hakko Kogyo Co., Asahimachi, Tokyo (Japan)

The recombinant B domain (FB) of staphylococcal protein A, which specifically binds to the Fc portion of immunoglobulin G (IgG), has been investigated with the use of two-dimensional proton nuclear magnetic resonance spectroscopy. All backbone and side-chain proton resonances of FB (60 amino acid residues), except the amide proton resonance of Ala2, were assigned by the sequential assignment procedures by using double-quantum-filtered correlated spectroscopy (DQF-COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA), and nuclear Overhauser enhancement spectroscopy (NOESY). On the basis of the NOESY data, three helical regions, Glu9-His19, Glu25-Asp37, and Ser42-Ala55, were identified in the free FB in solution. Existence of two of the three helical regions, Glu9-His19 and Glu25-Asp37, is consistent with the X-ray crystallographic structure of the Fc-bound FB. By contrast, in the Fc-bound FB as revealed by the X-ray analysis, the Ser42-Glu48 segment and no structural information has been available in the Ala49-Ala55 segment. The authors suggest that a significant conformation change is induced in the C-terminal region of FB when it is bound to the Fc portion of IgG.

OSTI ID:
5920959
Journal Information:
Biochemistry; (USA), Vol. 29:37; ISSN 0006-2960
Country of Publication:
United States
Language:
English