C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain
- Univ. of Maryland, Baltimore, MD (United States)
- Hare Research, Inc., Woodinville, WA (United States)
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.
- OSTI ID:
- 5077477
- Journal Information:
- Biochemistry; (United States), Vol. 30:25; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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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