| Autor: |
Mercado, Jonathan M., Lee, Sukyeong, Chang, Changsoo, Sung, Nuri, Soong, Lynn, Catic, Andre, Tsai, Francis T. F. |
| Zdroj: |
Proteins; Jun2022, Vol. 90 Issue 6, p1242-1246, 5p |
| Abstrakt: |
Hsp100 is an ATP‐dependent unfoldase that promotes protein disaggregation or facilitates the unfolding of aggregation‐prone polypeptides marked for degradation. Recently, new Hsp100 functions are emerging. In Plasmodium, an Hsp100 drives malaria protein export, presenting a novel drug target. Whether Hsp100 has a similar function in other protists is unknown. We present the 1.06 Å resolution crystal structure of the Hsp100 N‐domain from Leishmania spp., the causative agent of leishmaniasis in humans. Our structure reveals a network of methionines and aromatic amino acids that define the putative substrate‐binding site and likely evolved to protect Hsp100 from oxidative damage in host immune cells. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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