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

FEBS Letters

Waelchli, Markus²  Torigoe, Hidetaka¹  Sato, Moriyuki³  Shimada, Ichio¹  Arata, Yoji¹  Saito, Akiko³ 

[1] Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Hongo, Tokyo 113, Japan;Bruker Japan Co., Tsukuba, Ibaraki 305, Japan;Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Asahimachi 3-6-6, Machida, Tokyo 194, Japan

关键词: 15N-labeling;    Proline residue;    1H-15N HMBC;    Double labeling;    Recombinant B domain of protein A;    Immunoglobulin G;    FB;    B domain of Staphylococcal protein A;    Fc;    C-terminal half of the heavy chain of immunoglobulin;    HMBC;    1H-detected heteronuclear multiple bond correlation spectroscopy;    IgG;    immunoglobulin G;    DSS;    2;    2-dimethyl-2-silapentane-5-sulfonate;    HMQC;    1H-detected heteronuclear multiple quantum coherence spectroscopy;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(90)81147-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹⁵N nuclear magnetic resonance (NMR) studies of the B domain (FB) of Staphylococcus protein A, which is uniformly labeled with ¹⁵N, are reported. The α 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 the 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.

【 授权许可】

Unknown