Autor: |
Ferrer, Marc, Kapoor, Tarun M., Strassmaier, Tim, Weissenhorn, Winfried, Skehel, John J., Oprian, Dan, Schreiber, Stuart L., Wiley, Don C., Harrison, Stephen C. |
Předmět: |
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Zdroj: |
Nature Structural Biology; Oct99, Vol. 6 Issue 10, p953, 8p |
Abstrakt: |
The trimeric, α-helical coiled-coil core of the HIV-1 gp41 ectodomain is thought to be part of a transient, receptor-triggered intermediate in the refolding of the envelope glycoprotein into a fusion-active conformation. In an effort to discover small organic inhibitors that block gp41 activation, we have generated a biased combinatorial chemical library of non-natural binding elements targeted to the gp41 core. From this library of 61,275 potential ligands, we have identified elements that, when covalently attached to a peptide derived from the gp41 outer-layer α-helix, contribute to the formation of a stable complex with the inner core and to inhibition of gp41-mediated cell fusion. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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