Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5505
pubmed:dateCreated
2001-3-1
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
291
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
884-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11229405-Amino Acid Sequence, pubmed-meshheading:11229405-Anti-HIV Agents, pubmed-meshheading:11229405-Carrier Proteins, pubmed-meshheading:11229405-Cell Line, pubmed-meshheading:11229405-Drug Design, pubmed-meshheading:11229405-Giant Cells, pubmed-meshheading:11229405-HIV Antibodies, pubmed-meshheading:11229405-HIV Envelope Protein gp41, pubmed-meshheading:11229405-HIV-1, pubmed-meshheading:11229405-Humans, pubmed-meshheading:11229405-Membrane Fusion, pubmed-meshheading:11229405-Molecular Sequence Data, pubmed-meshheading:11229405-Neutralization Tests, pubmed-meshheading:11229405-Peptide Fragments, pubmed-meshheading:11229405-Peptides, pubmed-meshheading:11229405-Protein Conformation, pubmed-meshheading:11229405-Protein Folding, pubmed-meshheading:11229405-Protein Structure, Secondary, pubmed-meshheading:11229405-Tumor Cells, Cultured
pubmed:year
2001
pubmed:articleTitle
Protein design of an HIV-1 entry inhibitor.
pubmed:affiliation
Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. kimadmin@wi.mit.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.