1메가 달톤 크기 샤페로닌의 열린 그리고 닫힌 상태의 결정 구조

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 work, the two crystal structures of a chaperonin were determined 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 work, the two crystal structures of a chaperonin were determined to depict the molecular mechanism underpinning the mechanical motion of this protein machine.