Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA

Nat Struct Biol. 1997 Aug;4(8):605-8. doi: 10.1038/nsb0897-605.

Abstract

The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • DNA / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Lysine / chemistry
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Peptide Fragments / chemistry*
  • Protein Conformation
  • Transcription Factor TFIIIA
  • Transcription Factors / chemistry*
  • Zinc Fingers*

Substances

  • DNA-Binding Proteins
  • Peptide Fragments
  • Transcription Factor TFIIIA
  • Transcription Factors
  • DNA
  • Lysine