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Open AccessJournal ArticleDOI

Binding of the HIV-1 Nucleocapsid Protein to the Primer tRNALys3, inVitro, Is Essentially Not Specific

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TLDR
The data strongly suggested an essentially nonspecific binding of NCp7 to tRNA3 and thus did not seem to support a direct role ofNCp7, per se, in the selection of t RNA3 from the pool of cellular tRNAs.
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This article is published in Journal of Biological Chemistry.The article was published on 1995-01-27 and is currently open access. It has received 78 citations till now. The article focuses on the topics: Binding site & Low protein.

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Book ChapterDOI

Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism.

TL;DR: This chapter describes the effect of NC on individual steps in viral DNA synthesis and summarizes what is known about NC structure, NC nucleic acid binding properties, and the contribution of the zinc fingers to chaperone activity.
Journal ArticleDOI

Primer tRNAs for Reverse Transcription

TL;DR: A comparison of processes occurring in LTR retrotransposon primer tRNAs with similar processes occurs in retroviruses is also informative and is included herein.
Journal ArticleDOI

Cystatins in health and disease

TL;DR: This review focusses on the possible role of the cystatins, natural and specific inhibitors of the Cysteine proteinases, in pathological processes.
Journal ArticleDOI

Flexible Nature and Specific Functions of the HIV-1 Nucleocapsid Protein

TL;DR: The flexible nature of NC protein is presented, how it interacts with nucleic acids via its invariant zinc fingers and flanking basic residues, and the possible mechanisms that account for its multiple functions in the early steps of virus replication are presented.
Journal ArticleDOI

Structure of the complex between the HIV-1 nucleocapsid protein NCp7 and the single-stranded pentanucleotide d(ACGCC)

TL;DR: A mechanism of action for NCp7 in virus morphogenesis and replication is proposed from these results, which could facilitate the design of possible antiviral agents acting by a new mechanism.
References
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Journal ArticleDOI

Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.

TL;DR: The results indicate that the binding of any non-interacting ligand covering more than one lattice residue results in non- linear (convex downward) Scatchard plots, and the introduction of positive ligand-ligand co-operativity antagonizes this non-linearity, and eventually leads to plots of the opposite curvature.
Journal ArticleDOI

Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity.

TL;DR: The purpose of this review is to examine the various effects of low- molecular-weight electrolytes on the associations and interactions of proteins and nucleic acids through general electrostatic effects rather than chemical effects of particular ions.
Journal ArticleDOI

Potential metal-binding domains in nucleic acid binding proteins.

TL;DR: Observations suggest numerous experiments are needed to determine whether metal-binding domains are present in proteins and, if present, what roles such domains play in the processes of nucleic acid binding and gene regulation.
Journal ArticleDOI

Ion effects on ligand-nucleic acid interactions

TL;DR: The dominant factor driving complex formation between these charged ligands and the nucleic acid is the entropic contribution from the release of counterions, which appears to drive the non-specific interactions of proteins with nucleic acids.
Journal ArticleDOI

RNA double-helical fragments at atomic resolution. II. The crystal structure of sodium guanylyl-3',5'-cytidine nonahydrate.

TL;DR: The crystal structure of sodium guanylyl-3′,5′-cytidine (GpC) nonahydrate has been determined by X-ray diffraction procedures and refined to an R value of 0.054 and exhibits face-sharing octahedral co-ordination.
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