NMR paper Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR.

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[NMR paper] Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR.

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NMR processing:

MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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FANDAS

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V-NMR

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Backbone S2

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Camshift

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ArShift- Aromatic

ShiftS

Proshift

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CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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01-19-2018, 08:57 PM

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Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR.

Related Articles Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR.

Angew Chem Int Ed Engl. 2018 Jan 18;:

Authors: Deshmukh L, Tugarinov V, Appella DH, Clore GM

Abstract
HIV-1 nucleocapsid (NCp7) is a two Cys2HisCys zinc knuckle (N-Zn and C-Zn) protein that plays a key role in viral replication. Here we characterize NCp7 conformational dynamics by NMR relaxation dispersion and chemical exchange saturation transfer measurements. While the N-Zn knuckle is conformationally stable, the C-Zn knuckle interconverts on the millisecond time scale between the major state, in which the zinc is coordinated by three cysteines and a histidine, and two folded minor species (with populations around 1%) in which one of the coordination bonds (Cys413-S?---Zn or His421-N?2---Zn) is hydrolysed. These findings explain why anti-retroviral thioesters specifically disrupt the C-Zn knuckle by initial acylation of Cys413, and show that transient, sparsely-populated ('dark'), excited states of proteins can present effective targets for rational drug design.

PMID: 29345807 [PubMed - as supplied by publisher]

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