THE ZINC FINGER MOTIF - CONSERVATION OF CHEMICAL-SHIFTS AND CORRELATION WITH STRUCTURE

被引：28

作者：

LEE, MS ^{[1
]}

MORTISHIRESMITH, RJ ^{[1
]}

WRIGHT, PE ^{[1
]}

机构：

[1] UNIV CALIF SAN DIEGO,SCRIPPS INST OCEANOG,DEPT MOLEC BIOL,10666 N TORREY PINES RD,LA JOLLA,CA 92093

来源：

FEBS LETTERS | 1992年 / 309卷 / 01期

关键词：

ZINC FINGER; SECONDARY CHEMICAL SHIFT; CONSERVATION;

D O I：

10.1016/0014-5793(92)80732-V

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：

Zinc fingers of the transcription factor IIIA (TFIIIA) type, in which zinc is co-ordinated by two cysteine and two histidine ligands (Cys2/His2), contain a length of helix packed against a beta-hairpin. These zinc fingers comprise the widest range of structurally homologous proteins for which H-1 chemical shifts are available. A number of key resonances have chemical shifts that are highly sensitive to tertiary structure and are conserved between these peptides. The high conservation of these fingerprint chemical shifts is correlated with the common global fold of Cys2/His2 zinc fingers. These chemical shifts are largely independent of primary structure and should facilitate NMR assignments for future zinc finger proteins, as well as provide a diagnostic signature for the characteristic Cys2/His2 zinc finger fold.

引用

页码：29 / 32

页数：4

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