Zinc Folds the N-Terminal Domain of HIV-1 Integrase, Promotes Multimerization, and Enhances Catalytic Activity

Proceedings of the National Academy of Sciences of the United States of America- United States

doi 10.1073/pnas.93.24.13659

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Date

November 26, 1996

Authors

R. Zheng

T. M. Jenkins

R. Craigie

Publisher

Proceedings of the National Academy of Sciences

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Zinc Folds the N-Terminal Domain of HIV-1 Integrase, Promotes Multimerization, and Enhances Catalytic Activity

Proceedings of the National Academy of Sciences of the United States of America- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Characterization of Anti-Hiv Activity Mediated by HIV-1 Integrase C-Terminal Domain Polypeptides Expressed in Susceptible Cells

Large-Scale Conformational Dynamics of the HIV-1 Integrase Core Domain and Its Catalytic Loop Mutants

Truncation of N- And C-Terminal Regions of Streptococcus Mutans Dextranase Enhances Catalytic Activity

N-Terminal Half of Transportin SR2 Interacts With HIV Integrase

Structure of the HIV-1 Integrase Catalytic Domain Complexed With an Inhibitor: A Platform for Antiviral Drug Design

N-Terminal Syndecan-2 Domain Selectively Enhances 6-O Heparan Sulfate Chains Sulfation and Promotes VEGFA165-dependent Neovascularization

The Leucine-Rich Repeat Domain of Internalin B Folds Along a Polarized N-Terminal Pathway

Association of Mitochondrial Lysyl-tRNA Synthetase With HIV-1 GagPol Involves Catalytic Domain of the Synthetase and Transframe and Integrase Domains of Pol

HIV-1 Virus Interactions With Host Proteins: Interaction of the N-Terminal Domain of the HIV-1 Capsid Protein With Human Calmodulin