15N nuclear magnetic resonance studies of the B domain of staphylococcal protein A: sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobulin G.
15N nuclear magnetic resonance (NMR) studies of the B domain (FB) of Staphylococcus protein A, which is uniformly labeled with 15N, are reported. The alpha CH(i)-15N(i) connectivity in the 1H-15N HMBC spectrum and the 13C(i-1)-15N(i) spin coupling in the 15N spectrum of a 13C-, 15N-doubly labeled FB were used to establish the assignments of the imide 15N resonances for all three Pro residues that exist in FB. Addition of human IgG caused a significant downfield shift of the Pro-39 resonance. This result is quite consistent with our previous suggestion that a significant conformation change is induced in the Ser-42-Ala-55 helical region of FB when it is bound to human IgG.
Torigoe
H
H
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Shimada
I
I
Waelchli
M
M
Saito
A
A
Sato
M
M
Arata
Y
Y
D001665:Binding Sites; D006801:Humans; D007094:Imides; D007074:Immunoglobulin G / Q000378:metabolism / Q000648:ultrastructure*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D011392:Proline; D011487:Protein Conformation; D013205:Staphylococcal Protein A / Q000378:metabolism / Q000648:ultrastructure*
D007094:Imides; D007074:Immunoglobulin G; D013205:Staphylococcal Protein A; D011392:Proline