C terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain
Journal Article
·
· Biochemistry; (United States)
- 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), Journal Name: Biochemistry; (United States) Vol. 30:25; ISSN 0006-2960; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
Similar Records
High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach
Spectroscopic studies of wild-type and mutant zinc finger peptides: Determinants of domain folding and structure
ADR1a, a zinc finger peptide, exists in two folded conformations
Journal Article
·
Mon Jan 15 23:00:00 EST 1990
· Biochemistry; (USA)
·
OSTI ID:6698082
Spectroscopic studies of wild-type and mutant zinc finger peptides: Determinants of domain folding and structure
Journal Article
·
Sun Dec 31 23:00:00 EST 1989
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
·
OSTI ID:6810841
ADR1a, a zinc finger peptide, exists in two folded conformations
Journal Article
·
Tue Apr 09 00:00:00 EDT 1991
· Biochemistry; (United States)
·
OSTI ID:5595082
Related Subjects
550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
BARYONS
CHEMICAL SHIFT
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HEAVY WATER
HYDROGEN COMPOUNDS
MAGNETIC RESONANCE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
NUCLEOPROTEINS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
OXYGEN COMPOUNDS
PROTEINS
PROTONS
RESONANCE
TEMPERATURE DEPENDENCE
WATER
ZINC COMPOUNDS
62 RADIOLOGY AND NUCLEAR MEDICINE
BARYONS
CHEMICAL SHIFT
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HEAVY WATER
HYDROGEN COMPOUNDS
MAGNETIC RESONANCE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
NUCLEOPROTEINS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
OXYGEN COMPOUNDS
PROTEINS
PROTONS
RESONANCE
TEMPERATURE DEPENDENCE
WATER
ZINC COMPOUNDS