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Literature summary for 3.4.23.16 extracted from
- Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease (2008), Proteins, 70, 678-694.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme in complex with GADIFYLDGA, GAEVFYVDGA or GAQTFYVDGA | Human immunodeficiency virus 1 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| GADIFYLDGA | - |
Human immunodeficiency virus 1 |  |
| GAEVFYVDGA | - |
Human immunodeficiency virus 1 | |
| GAQTFYVDGA | - |
Human immunodeficiency virus 1 | |
| additional information | computational techniques to improve binding affinity are successfully applied to design peptide sequences that bind tighter to inactivated (D25N) HIV-1 protease | Human immunodeficiency virus 1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
- |
- |
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Release 2023.1 (January 2023)
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