Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

H-1, n-15 and c-13 resonance assignments for the first 3 zinc fingers of transcription factor iiia

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Liao, X. B.
  • Clemens, K.
  • Cavanagh, J.
  • Tennant, L.
  • Wright, Peter

publication date

  • May 1994

journal

  • Journal of Biomolecular NMR  Journal

abstract

  • The first three zinc fingers (ZF1-3) of transcription factor IIIA (TFIIIA) from Xenopus have been shown to contribute the majority of the binding energy to the intact TFIIIA-DNA interaction [Liao et al. (1992) J. Mol. Biol., 223, 857-871]. We have expressed a 92-amino acid polypeptide containing the three N-terminal zinc fingers of TFIIIA. This three-fingered polypeptide has been isotopically labeled with 15N and 13C in E. coli and purified to homogeneity. Assignment of backbone 1H, 15N, aliphatic 1H and 13C and aromatic 1H and 13C resonances of delta NZF1-3 has been obtained using a combination of single-, double- and triple-resonance multidimensional NMR experiments. The secondary structures for each finger have been determined from NOE connectivities, 3JNH alpha values and chemical shifts. The results show that each finger folds into a canonical beta-sheet-helix zinc finger structural motif, while the linkers adopt an extended structure. The helix between the two histidine ligands in ZF3 is distorted by zinc coordination, to accommodate the presence of four intervening amino acids instead of three as in ZF1 and ZF2.

subject areas

  • Amino Acid Sequence
  • Animals
  • Carbon Isotopes
  • Conserved Sequence
  • Histidine
  • Hydrogen
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Protein Structure, Secondary
  • RNA, Ribosomal, 5S
  • Transcription Factor TFIIIA
  • Transcription Factors
  • Xenopus
  • Zinc Fingers
scroll to property group menus

Research

keywords

  • NMR
  • STRUCTURE
  • TFIIIA
  • ZINC FINGER
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0925-2738

PubMed ID

  • 8019145
scroll to property group menus

Additional Document Info

start page

  • 433

end page

  • 454

volume

  • 4

issue

  • 3

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support