분자량 100만인 거대 단백질 복합체의 구조 연구

Abstract

Proteins mediate nearly all the biochemical reactions in cells and thus the proper protein folding is essential for the survival of cells. Accumulation of misfolded and denatured proteins is engaged in the progression of several diseases including neurodegeneration and cancer. Chaperonins (CPNs) play critical roles in proper folding of nascent proteins or in refolding of denature proteins. CPNs are multi-subunit complexes that have a folding chamber, and ATP-hydrolysis allosterically affects the conformation of CPNs to facilitate folding process. In this talk, I present the two crystal structures of a chaperonin to depict the molecular mechanism underpinning the mechanical motion of this protein machine.cluding neurodegeneration and cancer. Chaperonins (CPNs) play critical roles in proper folding of nascent proteins or in refolding of denature proteins. CPNs are multi-subunit complexes that have a folding chamber, and ATP-hydrolysis allosterically affects the conformation of CPNs to facilitate folding process. In this talk, I present the two crystal structures of a chaperonin to depict the molecular mechanism underpinning the mechanical motion of this protein machine.