Folding Pathways for Initiator and Effector Procaspases from Computer Simulations
MetadataShow full item record
The folding pathways of procaspases 3, 7, and 8 have been studied using a Go-like Hamiltonian and molecular dynamics simulations coupled with a parallel tempering scheme. The folding pathways and the overall structures of procaspases 3 and 7 are similar, and are characterized by monomeric as well as dimeric folding intermediates in agreement with the available structural and thermochemical data. The folding pathway of procaspase 8, on the other hand, is characterized by a larger population of monomers and partially folded dimer intermediates, and only a relatively small population of folded dimer species. The most stable structure predicted for procaspase 8 is a dimer,in which the position of the linker is remarkably different from the one observed in procaspases 3 and 7, leading to the fact that all the contacts that stabilize the active site are essentially formed. This novel and unexpected structure provides a rationale for the observed activity of the procaspase 8 dimer, and thus could be highly relevant for the initiation of FAS-mediated apoptosis. Proteins 2005;59:765-772.(c)2005 Wiley-Liss, Inc.
Copyright 2005 John Wiley & Sons, Ltd.
Please refer to the publisher for the definitive published version.
Showing items related by title, author, creator and subject.
Identification of residues involved in NS2 homodimerization and elucidation of their impact on the HCV life cycleGorzin, A.; Ramsland, Paul; Tachedjian, G.; Gowans, E. (2012)The NS2 protein of hepatitis C virus (HCV) plays a critical role in virus morphogenesis and infectivity. The crystal structure of the C-terminus of the NS2 protein (NS2 Pro) from the H77 strain ...
Schumann-Gillett, A.; Mark, A.; Deplazes, Evelyne; O'Mara, M. (2017)E-cadherin is a transmembrane glycoprotein that facilitates inter-cellular adhesion in the epithelium. The ectodomain of the native structure is comprised of five repeated immunoglobulin-like domains. All E-cadherin crystal ...
S-Nitrosated human serum albumin dimer as novel nano-EPR enhancer applied to macromolecular anti-tumor drugs such as micelles and liposomesKinoshita, R.; Ishima, Y.; Ikeda, M.; Kragh-Hansen, U.; Fang, J.; Nakamura, H.; Chuang, Victor; Tanaka, R.; Maeda, H.; Kodama, A.; Watanabe, H.; Maeda, H.; Otagiri, M.; Maruyama, T. (2015)© 2015 Elsevier B.V. All rights reserved. The enhanced permeability and retention (EPR) effect is a unique phenomenon of solid tumors, and it can serve as a basis for the development of macromolecular anticancer therapy. ...