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Title: C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain

Abstract

Two-dimensional NMR spectroscopic and computational methods were employed for the structure determination of an 18-residue peptide with the amino acid sequence of the C-terminal retriviral-type (r.t.) zinc finger domain from the nucleocapsid protein (NCP) of HIV-1 (Zn(HIV1-F2)). Unlike results obtained for the first retroviral-type zinc finger peptide, Zn (HIV1-F1) broad signals indicative of confomational lability were observed in the {sup 1}H NMR spectrum of An(HIV1-F2) at 25 C. The NMR signals narrowed upon cooling to {minus}2 C, enabling complete {sup 1}H NMR signal assignment via standard two-dimensional (2D) NMR methods. Distance restraints obtained from qualitative analysis of 2D nuclear Overhauser effect (NOESY) data were sued to generate 30 distance geometry (DG) structures with penalties in the range 0.02-0.03 {angstrom}{sup 2}. All structures were qualitatively consistent with the experimental NOESY spectrum based on comparisons with 2D NOESY back-calculated spectra. These results indicate that the r.t. zinc finger sequences observed in retroviral NCPs, simple plant virus coat proteins, and in a human single-stranded nucleic acid binding protein share a common structural motif.

Authors:
;  [1]; ;  [2]
  1. Univ. of Maryland, Baltimore, MD (United States)
  2. Hare Research, Inc., Woodinville, WA (United States)
Publication Date:
OSTI Identifier:
5077477
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 30:25; Journal ID: ISSN 0006-2960
Country of Publication:
United States
Language:
English
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; NUCLEOPROTEINS; NUCLEAR MAGNETIC RESONANCE; CHEMICAL SHIFT; HEAVY WATER; OVERHAUSER EFFECT; PROTONS; TEMPERATURE DEPENDENCE; ZINC COMPOUNDS; BARYONS; ELEMENTARY PARTICLES; FERMIONS; HADRONS; HYDROGEN COMPOUNDS; MAGNETIC RESONANCE; NUCLEONS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PROTEINS; RESONANCE; WATER; 550601* - Medicine- Unsealed Radionuclides in Diagnostics

Citation Formats

South, T L, Blake, P R, Hare, D R, and Summers, M F. C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain. United States: N. p., 1991. Web. doi:10.1021/bi00239a036.
South, T L, Blake, P R, Hare, D R, & Summers, M F. C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain. United States. https://doi.org/10.1021/bi00239a036
South, T L, Blake, P R, Hare, D R, and Summers, M F. Tue . "C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain". United States. https://doi.org/10.1021/bi00239a036.
@article{osti_5077477,
title = {C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain},
author = {South, T L and Blake, P R and Hare, D R and Summers, M F},
abstractNote = {Two-dimensional NMR spectroscopic and computational methods were employed for the structure determination of an 18-residue peptide with the amino acid sequence of the C-terminal retriviral-type (r.t.) zinc finger domain from the nucleocapsid protein (NCP) of HIV-1 (Zn(HIV1-F2)). Unlike results obtained for the first retroviral-type zinc finger peptide, Zn (HIV1-F1) broad signals indicative of confomational lability were observed in the {sup 1}H NMR spectrum of An(HIV1-F2) at 25 C. The NMR signals narrowed upon cooling to {minus}2 C, enabling complete {sup 1}H NMR signal assignment via standard two-dimensional (2D) NMR methods. Distance restraints obtained from qualitative analysis of 2D nuclear Overhauser effect (NOESY) data were sued to generate 30 distance geometry (DG) structures with penalties in the range 0.02-0.03 {angstrom}{sup 2}. All structures were qualitatively consistent with the experimental NOESY spectrum based on comparisons with 2D NOESY back-calculated spectra. These results indicate that the r.t. zinc finger sequences observed in retroviral NCPs, simple plant virus coat proteins, and in a human single-stranded nucleic acid binding protein share a common structural motif.},
doi = {10.1021/bi00239a036},
url = {https://www.osti.gov/biblio/5077477}, journal = {Biochemistry; (United States)},
issn = {0006-2960},
number = ,
volume = 30:25,
place = {United States},
year = {1991},
month = {6}
}