Programa del Ciclo de Seminarios del IQFR 2014
Seminario del Dr. Guillermo Montoya
Centro Nacional de Investigaciones Oncológicas
"Structural insights into the the TRiC/CCT complex function and mechanism"
Martes 25 de marzo a las 12:00 horas
Aula 300 IQFR-CSIC
Resumen:
CCT (chaperonin containing TCP-1, also know as TRiC) is a molecular machine that forms a high molecular weight complex (1000 KDa). CCT has crucial relevance in several important biological processes and is emerging as a key molecule during mitosis due to its essential role in the folding of many important proteins involved in cell division Cdh1,Plk1, p27, Cdc20, PP2a, tubulin or actin). Therefore this complex is a possible antitumoral target due to its regulation of crucial processes in cell division. The assembly is formed by eight different subunits called CCTα, β, γ, δ, ε, ζ, η and θ in mammals corresponding to CCT1–8 in yeast. All chaperonins display an open substrate-receptive conformation, where the unfolded protein is recognized and trapped, and a closed conformation where the substrate is isolated from the bulk of the intracellular environment.
The transition between the open and closed states is induced upon ATP binding and hydrolysis, and triggers a complex set of intra- and inter-ring allosteric.
We successfully solved the structure of the open CCT complex including tubulin as a bound substrate at 5.5 Å resolution. Using a hybrid approach we have suggested a new working model for this protein complex.
Dirección y como llegar
Fuente:
www.iqfr.csic.es
CCT (chaperonin containing TCP-1, also know as TRiC) is a molecular machine that forms a high molecular weight complex (1000 KDa). CCT has crucial relevance in several important biological processes and is emerging as a key molecule during mitosis due to its essential role in the folding of many important proteins involved in cell division Cdh1,Plk1, p27, Cdc20, PP2a, tubulin or actin). Therefore this complex is a possible antitumoral target due to its regulation of crucial processes in cell division. The assembly is formed by eight different subunits called CCTα, β, γ, δ, ε, ζ, η and θ in mammals corresponding to CCT1–8 in yeast. All chaperonins display an open substrate-receptive conformation, where the unfolded protein is recognized and trapped, and a closed conformation where the substrate is isolated from the bulk of the intracellular environment.
The transition between the open and closed states is induced upon ATP binding and hydrolysis, and triggers a complex set of intra- and inter-ring allosteric.
We successfully solved the structure of the open CCT complex including tubulin as a bound substrate at 5.5 Å resolution. Using a hybrid approach we have suggested a new working model for this protein complex.
Dirección y como llegar
Fuente:
www.iqfr.csic.es
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