| pubmed-article:9861018 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0205402 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C1510420 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C2346874 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0913822 | lld:lifeskim |
| pubmed-article:9861018 | lifeskim:mentions | umls-concept:C0913823 | lld:lifeskim |
| pubmed-article:9861018 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:9861018 | pubmed:dateCreated | 1999-1-28 | lld:pubmed |
| pubmed-article:9861018 | pubmed:abstractText | Synthetic C peptides, corresponding to the C helix of the HIV type 1 (HIV-1) gp41 envelope protein, are potent inhibitors of HIV-1 membrane fusion. One such peptide is in clinical trials. The crystal structure of the gp41 core, in its proposed fusion-active conformation, is a trimer of helical hairpins in which three C helices pack against a central coiled coil. Each C helix shows especially prominent contacts with one of three symmetry-related, hydrophobic cavities on the surface of the coiled coil. We show that the inhibitory activity of the C peptide C34 depends on its ability to bind to this coiled-coil cavity. Moreover, examining a series of C34 peptide variants with modified cavity-binding residues, we find a linear relationship between the logarithm of the inhibitory potency and the stability of the corresponding helical-hairpin complexes. Our results provide strong evidence that this coiled-coil cavity is a good drug target and clarify the mechanism of C peptide inhibition. They also suggest simple, quantitative assays for the identification and evaluation of analogous inhibitors of HIV-1 entry. | lld:pubmed |
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| pubmed-article:9861018 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9861018 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9861018 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9861018 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9861018 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9861018 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9861018 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9861018 | pubmed:author | pubmed-author:ChanD CDC | lld:pubmed |
| pubmed-article:9861018 | pubmed:author | pubmed-author:KimP SPS | lld:pubmed |
| pubmed-article:9861018 | pubmed:author | pubmed-author:ChutkowskiC... | lld:pubmed |
| pubmed-article:9861018 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9861018 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:9861018 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9861018 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9861018 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9861018 | pubmed:pagination | 15613-7 | lld:pubmed |
| pubmed-article:9861018 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9861018 | pubmed:meshHeading | pubmed-meshheading:9861018-... | lld:pubmed |
| pubmed-article:9861018 | pubmed:meshHeading | pubmed-meshheading:9861018-... | lld:pubmed |
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| pubmed-article:9861018 | pubmed:meshHeading | pubmed-meshheading:9861018-... | lld:pubmed |
| pubmed-article:9861018 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9861018 | pubmed:articleTitle | Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. | lld:pubmed |
| pubmed-article:9861018 | pubmed:affiliation | Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142, USA. | lld:pubmed |
| pubmed-article:9861018 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9861018 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
