| Protein design of an HIV-1 entry inhibitor. | |
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MedLine Citation:
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PMID: 11229405 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Human immunodeficiency virus type-1 (HIV-1) membrane fusion is promoted by the formation of a trimer-of-hairpins structure that brings the amino- and carboxyl-terminal regions of the gp41 envelope glycoprotein ectodomain into close proximity. Peptides derived from the carboxyl-terminal region (called C-peptides) potently inhibit HIV-1 entry by binding to the gp41 amino-terminal region. To test the converse of this inhibitory strategy, we designed a small protein, denoted 5-Helix, that binds the C-peptide region of gp41. The 5-Helix protein displays potent (nanomolar) inhibitory activity against diverse HIV-1 variants and may serve as the basis for a new class of antiviral agents. The inhibitory activity of 5-Helix also suggests a strategy for generating an HIV-1 neutralizing antibody response that targets the carboxyl-terminal region of the gp41 ectodomain. |
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Authors:
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M J Root; M S Kay; P S Kim |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Science (New York, N.Y.) Volume: 291 ISSN: 0036-8075 ISO Abbreviation: Science Publication Date: 2001 Feb |
Date Detail:
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Created Date: 2001-03-01 Completed Date: 2001-03-08 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0404511 Medline TA: Science Country: United States |
Other Details:
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Languages: eng Pagination: 884-8 Citation Subset: IM |
Affiliation:
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Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. kimadmin@wi.mit.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Anti-HIV Agents* / chemistry, immunology, metabolism, pharmacology Carrier Proteins / chemistry*, metabolism, pharmacology* Cell Line Drug Design* Giant Cells / drug effects HIV Antibodies / immunology HIV Envelope Protein gp41 / chemistry, metabolism* HIV-1 / drug effects*, physiology Humans Membrane Fusion / drug effects* Molecular Sequence Data Neutralization Tests Peptide Fragments / chemistry, immunology, metabolism Peptides* Protein Conformation Protein Folding Protein Structure, Secondary Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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P01 GM56552/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/5-helix protein, synthetic; 0/Anti-HIV Agents; 0/Carrier Proteins; 0/HIV Antibodies; 0/HIV Envelope Protein gp41; 0/Peptide Fragments; 0/Peptides |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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