Načítá se...
The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 Å resolution
Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC(50) = 0.62 µM) based on a reduced-bond transition...
Uloženo v:
| Hlavní autoři: | , , |
|---|---|
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2013
|
| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3943106/ https://ncbi.nlm.nih.gov/pubmed/24419612 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X13032974 |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!
|