The long term goal of this NIH NIAID funded project is to gain a mechanistic understanding of Mycobacterium tuberculosis proteostasis as exemplified by the Mtb Pup-proteasome system and the Mtb DnaK-ClpB system, and to use the structure-function knowledge to develop anti-TB agents.
Cryo-EM structure of the Mycobacterium tuberculosis (Mtb) ClpB hexamer. No high-resolution structure exits in literature for a hexameric protein dis-aggregating ATPase. We study this protein and its inhibitor development in the context of Mtb proteo-stasis, which encompasses protein degradation by the Mtb Pup-proteasome system, and the protein rescue/disaggregation system the Mtb DnaK-ClpB system. Mtb survives in the hash environment of its host immune cells the macrophage by fine tuning the two systems
The long term goal of this NIH NIAID funded project is to gain a mechanistic understanding of Mycobacterium tuberculosis proteostasis as exemplified by the Mtb Pup-proteasome system and the Mtb DnaK-ClpB system, and to use the structure-function knowledge to develop anti-TB agents.
Cryo-EM structure of the Mycobacterium tuberculosis (Mtb) ClpB hexamer. No high-resolution structure exits in literature for a hexameric protein dis-aggregating ATPase. We study this protein and its inhibitor development in the context of Mtb proteo-stasis, which encompasses protein degradation by the Mtb Pup-proteasome system, and the protein rescue/disaggregation system the Mtb DnaK-ClpB system. Mtb survives in the hash environment of its host immune cells the macrophage by fine tuning the two systems
The long term goal of this NIH NIAID funded project is to gain a mechanistic understanding of Mycobacterium tuberculosis proteostasis as exemplified by the Mtb Pup-proteasome system and the Mtb DnaK-ClpB system, and to use the structure-function knowledge to develop anti-TB agents.
Cryo-EM structure of the Mycobacterium tuberculosis (Mtb) ClpB hexamer. No high-resolution structure exits in literature for a hexameric protein dis-aggregating ATPase. We study this protein and its inhibitor development in the context of Mtb proteo-stasis, which encompasses protein degradation by the Mtb Pup-proteasome system, and the protein rescue/disaggregation system the Mtb DnaK-ClpB system. Mtb survives in the hash environment of its host immune cells the macrophage by fine tuning the two systems
The long term goal of this NIH NIAID funded project is to gain a mechanistic understanding of Mycobacterium tuberculosis proteostasis as exemplified by the Mtb Pup-proteasome system and the Mtb DnaK-ClpB system, and to use the structure-function knowledge to develop anti-TB agents.
Cryo-EM structure of the Mycobacterium tuberculosis (Mtb) ClpB hexamer. No high-resolution structure exits in literature for a hexameric protein dis-aggregating ATPase. We study this protein and its inhibitor development in the context of Mtb proteo-stasis, which encompasses protein degradation by the Mtb Pup-proteasome system, and the protein rescue/disaggregation system the Mtb DnaK-ClpB system. Mtb survives in the hash environment of its host immune cells the macrophage by fine tuning the two systems