rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
6
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pubmed:dateCreated |
2005-6-3
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pubmed:databankReference |
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pubmed:abstractText |
Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding partner of HIV-1 integrase (IN) in human cells. We have determined the NMR structure of the integrase-binding domain (IBD) in LEDGF and identified amino acid residues essential for the interaction. The IBD is a compact right-handed bundle composed of five alpha-helices. Based on folding topology, the IBD is structurally related to a diverse family of alpha-helical proteins that includes eukaryotic translation initiation factor eIF4G and karyopherin-beta. LEDGF residues essential for the interaction with IN were localized to interhelical loop regions of the bundle structure. Interaction-defective IN mutants were previously shown to cripple replication although they retained catalytic function. The initial structure determination of a host cell factor that tightly binds to a retroviral enzyme lays the groundwork for understanding enzyme-host interactions important for viral replication.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
1545-9993
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
526-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15895093-Amino Acid Sequence,
pubmed-meshheading:15895093-Animals,
pubmed-meshheading:15895093-Binding Sites,
pubmed-meshheading:15895093-Cloning, Molecular,
pubmed-meshheading:15895093-Fibroblast Growth Factors,
pubmed-meshheading:15895093-Growth Substances,
pubmed-meshheading:15895093-HIV Integrase,
pubmed-meshheading:15895093-HIV-1,
pubmed-meshheading:15895093-Humans,
pubmed-meshheading:15895093-Magnetic Resonance Spectroscopy,
pubmed-meshheading:15895093-Mammals,
pubmed-meshheading:15895093-Models, Molecular,
pubmed-meshheading:15895093-Molecular Sequence Data,
pubmed-meshheading:15895093-Mutagenesis,
pubmed-meshheading:15895093-Open Reading Frames,
pubmed-meshheading:15895093-Protein Structure, Secondary,
pubmed-meshheading:15895093-Recombinant Proteins,
pubmed-meshheading:15895093-Restriction Mapping
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pubmed:year |
2005
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pubmed:articleTitle |
Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75.
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pubmed:affiliation |
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, 44 Binney Street, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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