Ontology type: schema:ScholarlyArticle Open Access: True
2014-01
AUTHORSDavid Schwefel, Harriet C. T. Groom, Virginie C. Boucherit, Evangelos Christodoulou, Philip A. Walker, Jonathan P. Stoye, Kate N. Bishop, Ian A. Taylor
ABSTRACTLentiviruses contain accessory genes that have evolved to counteract the effects of host cellular defence proteins that inhibit productive infection. One such restriction factor, SAMHD1, inhibits human immunodeficiency virus (HIV)-1 infection of myeloid-lineage cells as well as resting CD4(+) T cells by reducing the cellular deoxynucleoside 5'-triphosphate (dNTP) concentration to a level at which the viral reverse transcriptase cannot function. In other lentiviruses, including HIV-2 and related simian immunodeficiency viruses (SIVs), SAMHD1 restriction is overcome by the action of viral accessory protein x (Vpx) or the related viral protein r (Vpr) that target and recruit SAMHD1 for proteasomal degradation. The molecular mechanism by which these viral proteins are able to usurp the host cell's ubiquitination machinery to destroy the cell's protection against these viruses has not been defined. Here we present the crystal structure of a ternary complex of Vpx with the human E3 ligase substrate adaptor DCAF1 and the carboxy-terminal region of human SAMHD1. Vpx is made up of a three-helical bundle stabilized by a zinc finger motif, and wraps tightly around the disc-shaped DCAF1 molecule to present a new molecular surface. This adapted surface is then able to recruit SAMHD1 via its C terminus, making it a competent substrate for the E3 ligase to mark for proteasomal degradation. The structure reported here provides a molecular description of how a lentiviral accessory protein is able to subvert the cell's normal protein degradation pathway to inactivate the cellular viral defence system. More... »
PAGES234
http://scigraph.springernature.com/pub.10.1038/nature12815
DOIhttp://dx.doi.org/10.1038/nature12815
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"value": [
"10.1038/nature12815"
]
},
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1031756380"
]
}
],
"sameAs": [
"https://doi.org/10.1038/nature12815",
"https://app.dimensions.ai/details/publication/pub.1031756380"
],
"sdDataset": "articles",
"sdDatePublished": "2019-04-10T16:29",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8669_00000425.jsonl",
"type": "ScholarlyArticle",
"url": "https://www.nature.com/articles/nature12815"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/nature12815'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/nature12815'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/nature12815'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/nature12815'
This table displays all metadata directly associated to this object as RDF triples.
341 TRIPLES
21 PREDICATES
91 URIs
39 LITERALS
27 BLANK NODES