Kobuviral Non-structural 3A Proteins Act as Molecular Harnesses to Hijack the Host ACBD3 Protein

Structure

Volumn 25, Issue 2, 2017, Pages 219-230

  Klima, Martin ^a   Chalupska, Dominika ^a   Różycki, Bartosz ^b   Humpolickova, Jana ^a   Rezabkova, Lenka ^c   Silhan, Jan ^a   Baumlova, Adriana ^a   Dubankova, Anna ^a   Boura, Evzen ^a  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

^b INSTITUTE OF PHYSICS   (Poland)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

Author keywords

3A; ACBD3; Aichivirus; GOLD; Kobuvirus; molecular dynamics simulations; structure

Indexed keywords

ACYL COA BINDING DOMAIN PROTEIN 3; MORPHINE SULFATE; PROTEIN; SELENOMETHIONINE; UNCLASSIFIED DRUG; VIRAL PROTEIN; ACBD3 PROTEIN, HUMAN; LIPOSOME; MEMBRANE PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ARTICLE; ASSAY; BINDING ASSAY; BINDING SITE; BIOCHEMICAL ANALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALLOGRAPHY; DISSOCIATION CONSTANT; HYDROGEN BOND; HYDROPHOBICITY; IN VITRO STUDY; LIPID BILAYER; MEMBRANE BINDING; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEDIMENTATION; SEQUENCE HOMOLOGY; STOICHIOMETRY; SURFACE PLASMON RESONANCE; ULTRACENTRIFUGATION; ALPHA HELIX; BETA SHEET; CELL LINE; CHEMISTRY; GENE EXPRESSION; GENETICS; HOST PATHOGEN INTERACTION; HUMAN; KOBUVIRUS; METABOLISM; MOLECULAR CLONING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STABILITY; VIRUS REPLICATION; X RAY CRYSTALLOGRAPHY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID MOTIFS; BINDING SITES; CELL LINE; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; GENE EXPRESSION; HOST-PATHOGEN INTERACTIONS; HUMANS; KOBUVIRUS; MEMBRANE PROTEINS; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STABILITY; RECOMBINANT PROTEINS; UNILAMELLAR LIPOSOMES; VIRAL NONSTRUCTURAL PROTEINS; VIRUS REPLICATION;

EID: 85008424048     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.11.021     Document Type: Article

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