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Assessment of zinc finger orientations by residual dipolar coupling constants

Academic Article
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Overview

related to degree

  • Tsui, Vickie, Ph.D. in Biology, Scripps Research 1996 - 2001

authors

  • Tsui, Vickie
  • Zhu, L. M.
  • Huang, T. H.
  • Wright, Peter
  • Case, David A.

publication date

  • January 2000

journal

  • Journal of Biomolecular NMR  Journal

abstract

  • Residual dipolar coupling constants measured in anisotropic solution contain information on orientations between internuclear vectors and the magnetic field, providing long-range information that may help determine the relative orientations of distinct domains in biomolecules. Here we describe the measurement and use of residual dipolar coupling restraints in the refinement of the structure of the complex of DNA with three zinc fingers of transcription factor IIIA (TFIIIA), measured in a DMPC/DHPC bicelle solution. These dipolar restraints were applied on a variety of orientations of the zinc finger domains (derived from crystallography, previous NMR studies, and systematic modeling) in order to examine the validity and sensitivity of using residual dipolar splittings to study interdomain orientations. The spread in interdomain angles between zinc fingers is reduced from 24 degrees to 9 degrees upon incorporation of dipolar restraints. However, the results also show that the ability to determine relative orientations is strongly dependent on the structural accuracy of the local domain structures.

subject areas

  • Computer Simulation
  • DNA
  • DNA-Binding Proteins
  • Dimyristoylphosphatidylcholine
  • Models, Chemical
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Phospholipid Ethers
  • Solutions
  • Transcription Factor TFIIA
  • Transcription Factors
  • Zinc Fingers
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Research

keywords

  • dipolar couplings
  • domain orientation
  • transcription factor III A
  • zinc fingers
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Identity

International Standard Serial Number (ISSN)

  • 0925-2738

Digital Object Identifier (DOI)

  • 10.1023/a:1008302430561

PubMed ID

  • 10718608
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Additional Document Info

start page

  • 9

end page

  • 21

volume

  • 16

issue

  • 1

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