PROTON AND NITROGEN SEQUENTIAL ASSIGNMENTS AND SECONDARY STRUCTURE DETERMINATION OF THE HUMAN FK506 AND RAPAMYCIN BINDING-PROTEIN

被引：49

作者：

ROSEN, MK ^{[1
]}

MICHNICK, SW ^{[1
]}

KARPLUS, M ^{[1
]}

SCHREIBER, SL ^{[1
]}

机构：

[1] HARVARD UNIV, DEPT CHEM, 12 OXFORD ST, CAMBRIDGE, MA 02138 USA

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 19期

关键词：

D O I：

10.1021/bi00233a020

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：

Sequential H-1 and N-15 assignments of human FKBP, a cytosolic binding protein for the immunosuppressive agents FK506 and rapamycin, are reported. A combination of homonuclear and relayed heteronuclear experiments has enabled assignment of 98 of 99 backbone amide NHs, 119 of 120 C-alpha-Hs, 97 of 99 non-proline amide N-15(s), and 375 of 412 side-chain resonances of this 107-residue protein. Long-range NOEs are used to demonstrate that FKBP has a novel folding topology consisting of a five-stranded antiparallel beta-sheet with +3, +1, -3, +1 loop connectivity.

引用

页码：4774 / 4789

页数：16

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