N-15 NUCLEAR-MAGNETIC-RESONANCE STUDIES OF THE B-DOMAIN OF STAPHYLOCOCCAL PROTEIN-A - SEQUENCE SPECIFIC ASSIGNMENTS OF THE IMIDE N-15 RESONANCES OF THE PROLINE RESIDUES AND THE INTERACTION WITH HUMAN IMMUNOGLOBULIN-G

被引：18

作者：

TORIGOE, H

SHIMADA, I

WAELCHLI, M

SAITO, A

SATO, M

ARATA, Y

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN

[2] BRUKER JAPAN CO,TSUKUBA,IBARAKI 305,JAPAN

[3] KYOWA HAKKO KOGYO CO LTD,TOKYO RES LABS,MACHIDA,TOKYO 194,JAPAN

来源：

FEBS LETTERS | 1990年 / 269卷 / 01期

关键词：

!sup]15[!/sup]N-labeling; !sup]1[!/sup]H-[!sup]15[!/sup]N HMBC; Double labeling; Immunoglobulin G; Proline residue; Recombinant B domain of protein A;

D O I：

10.1016/0014-5793(90)81147-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. © 1990.

引用

页码：174 / 176

页数：3

共 17 条

[1] CORRELATION OF PROTON AND N-15 CHEMICAL-SHIFTS BY MULTIPLE QUANTUM NMR [J].