Zinc finger proteins: new insights into structural and functional diversity

Zinc finger proteins: new insights into structural and functional diversity Zinc finger proteins are among the most abundant proteins in eukaryotic genomes. Their functions are extraordinarily diverse and include DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding. Zinc finger structures are as diverse as their functions. Structures have recently been reported for many new zinc finger domains with novel topologies, providing important insights into structure/function relationships. In addition, new structural studies of proteins containing the classical Cys 2 His 2 zinc finger motif have led to novel insights into mechanisms of DNA binding and to a better understanding of their broader functions in transcriptional regulation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Structural Biology Elsevier

Zinc finger proteins: new insights into structural and functional diversity

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Publisher
Elsevier
Copyright
Copyright © 2001 Elsevier Science Ltd
ISSN
0959-440x
D.O.I.
10.1016/S0959-440X(00)00167-6
Publisher site
See Article on Publisher Site

Abstract

Zinc finger proteins are among the most abundant proteins in eukaryotic genomes. Their functions are extraordinarily diverse and include DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding. Zinc finger structures are as diverse as their functions. Structures have recently been reported for many new zinc finger domains with novel topologies, providing important insights into structure/function relationships. In addition, new structural studies of proteins containing the classical Cys 2 His 2 zinc finger motif have led to novel insights into mechanisms of DNA binding and to a better understanding of their broader functions in transcriptional regulation.

Journal

Current Opinion in Structural BiologyElsevier

Published: Feb 1, 2001

References

  • Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificity
    Wuttke, DS; Foster, MP; Case, DA; Gottesfeld, JM; Wright, PE
  • Advances in zinc finger engineering
    Choo, Y; Isalan, M
  • A dual role for zinc fingers in both DNA binding and zinc sensing by the zap1 transcriptional activator
    Bird, AJ; Zhao, H; Luo, H; Jensen, LT; Srinivasan, C; Evans-Galea, M; Winge, DR; Eide, DJ
  • Zinc finger domains: hypotheses and current knowledge
    Berg, JM
  • Aiolos, a lymphoid restricted transcription factor that interacts with Ikaros to regulate lymphocyte differentiation
    Morgan, B; Sun, L; Avitahl, N; Andrikopoulos, K; Ikeda, T; Gonzales, E; Wu, P; Neben, S; Georgopoulos, K
  • Transcriptional cofactors of the FOG family interact with GATA proteins by means of multiple zinc fingers
    Fox, AH; Liew, C; Holmes, M; Kowalski, K; Mackay, J; Crossley, M
  • Dynamical behavior of the HIV-1 nucleocapsid protein
    Lee, BM; De Guzman, RN; Turner, BG; Tjandra, N; Summers, MF
  • The solution structure of ribosomal protein L36 from Thermus thermophilus reveals a zinc-ribbon-like fold
    Hard, T; Rak, A; Allard, P; Kloo, L; Garber, M
  • Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ
    Martinez-Yamout, M; Legge, GB; Zhang, O; Wright, PE; Dyson, HJ
  • Phosphatidylinositol 3-phosphate recognition by the FYVE domain
    Kutateladze, TG; Ogburn, KD; Watson, WT; de Beer, T; Emr, SD; Burd, CG; Overduin, M
  • Structure of the PHD zinc finger from human Williams–Beuren syndrome transcription factor
    Pascual, J; Martinez-Yamout, M; Dyson, HJ; Wright, PE

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