Tyrosine phosphorylation induced by C4 peptide constructs from HIV Gp120
Treatment of HUT78 cells with CD4-binding peptide constructs derived from the C4 domain of HIV-1 gp120 results in autophosphorylation of a src-related kinase, p56 lck. This leads to p56 lck activation and the subsequent phosphorylation of tyrosine residues in several intracellular proteins. The phos...
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Published in | Peptides (New York, N.Y. : 1980) Vol. 20; no. 2; pp. 185 - 191 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.01.1999
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Subjects | |
Online Access | Get full text |
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Summary: | Treatment of HUT78 cells with CD4-binding peptide constructs derived from the C4 domain of HIV-1 gp120 results in autophosphorylation of a src-related kinase, p56
lck. This leads to p56
lck activation and the subsequent phosphorylation of tyrosine residues in several intracellular proteins. The phosphorylation is specific to the C4 peptides as no new phosphorylation occurs when the cells are treated with control peptides or polymers. The induction of tyrosine phosphorylation by the C4 peptide constructs depends on the capability of the peptide to assume a helical conformation because similar peptide constructs that were not able to form helices did not induce cellular tyrosine phosphorylation. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/S0196-9781(98)00158-2 |