pubmed-article:15895093 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1335268 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:15895093 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:15895093 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:15895093 | pubmed:dateCreated | 2005-6-3 | lld:pubmed |
pubmed-article:15895093 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15895093 | 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. | lld:pubmed |
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pubmed-article:15895093 | pubmed:language | eng | lld:pubmed |
pubmed-article:15895093 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15895093 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15895093 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15895093 | pubmed:month | Jun | lld:pubmed |
pubmed-article:15895093 | pubmed:issn | 1545-9993 | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:WagnerGerhard... | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:SunZhen-Yu... | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:CherepanovPet... | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:MaertensGoede... | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:EngelmanAlanA | lld:pubmed |
pubmed-article:15895093 | pubmed:author | pubmed-author:RahmanShailaS | lld:pubmed |
pubmed-article:15895093 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15895093 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:15895093 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15895093 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15895093 | pubmed:pagination | 526-32 | lld:pubmed |
pubmed-article:15895093 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:15895093 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15895093 | pubmed:articleTitle | Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75. | lld:pubmed |
pubmed-article:15895093 | pubmed:affiliation | Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, 44 Binney Street, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:15895093 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15895093 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15895093 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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