Nucleocapsid protein preferentially binds the stem-loop of duplex/quadruplex hybrid that unfolds the quadruplex structure

Abstract

Nucleic acids can form noncanonical structure of four-stranded G-quadruplex in addition to the duplex structures. Nucleocapsid protein 7 (NCp7) of HIV-1 virus can bind to a unique duplex/quadruplex structure (LTR-III),...

Structural elucidation of HIV-1 G-quadruplexes in a cellular environment and their ligand binding using responsive 19F-labeled nucleoside probes

“…[14][15][16] Importantly, the LTR GQ region represents an evolutionary conserved element across all primate lentiviruses, and the balance between different GQ structures is implicated in the propagation and latency of the virus. 17,18 Therefore, we envision that the virus status can be selectively controlled in the host cell by using structure-specic binders. In this direction, it is important to gain a comprehensive understanding of the structural polymorphism, dynamics and druggable space of LTR GQs in a cellular environment to advocate a viable therapeutic strategy.…”

Structural Antagonism‐Aided Conformational Regulation Enables an Aptamer‐Loop G‐Quadruplex Modular Sensor of β‐Lactoglobulin

“…As already reported for a hairpin-loop G-quadruplex (G4), it binds on functional protein via its hairpin loop, inducing structural and functional changes in the G4, i.e., disrupting the G4, causing dysfunctional DNA replication or stabilizing the hairpin-G4 to promote additional regulation. [20,21] Moreover, a G4 performs unique functions that depend on its nonclassical conformation. The G4 nucleic acid sequence comprises four consecutive guanine runs (G-runs) and three intervening short oligonucleotides.…”