1메가 달톤 크기 샤페로닌의 열린 그리고 닫힌 상태의 결정 구조

Title
1메가 달톤 크기 샤페로닌의 열린 그리고 닫힌 상태의 결정 구조
Alternative Title
Crystal structures of the open and closed states of a ~1 megadalton chaperonin
Author(s)
안영준; 차선신
KIOST Author(s)
Young, Jun An(안영준)
Alternative Author(s)
안영준
Publication Year
2016-09-22
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.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/24604
Bibliographic Citation
The 16th KIAS Conference on Protein Structure and Function, pp.63, 2016
Publisher
KIAS
Type
Conference
Language
English
Publisher
KIAS
Related Researcher
Research Interests

Structural biology,Protein Engineering,구조생물학,단백질 공학

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