Molecular determinants of the ATP hydrolysis asymmetry of the CCT chaperonin complex
Author:
Affiliation:
1. Computational Systems Biology Group; Centro Nacional de Biotecnología (CNB-CSIC); Darwin 3 28049 Madrid Spain
2. Department of Macromolecular Structure; Centro Nacional de Biotecnología (CNB-CSIC); Darwin 3 28049 Madrid Spain
Funder
Ministerio de Ciencia e Innovación (Spanish Ministry of Science and Innovation)
Comunidad de Madrid (Madrid Regional Government)
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference33 articles.
1. Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding;Horwich;Q Rev Biophys,2009
2. The substrate recognition mechanisms in chaperonins;Gomez-Puertas;J Mol Recognit,2004
3. Structure and Function of the Cytosolic Chaperonin CCT
4. Chaperonins: two rings for folding;Yebenes;Trends Biochem Sci,2011
5. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis;Rivenzon-Segal;Nat Struct Mol Biol,2005
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