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A study of the structural properties and thermal stability of human Bcl-2 by molecular dynamics simulations.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ilizaliturri-Flores, Ian Correa-Basurto, José Benítez-Cardoza, Claudia G. Zamorano-Carrillo, Absalom
Description	Country affiliation: Mexico Author Affiliation: Ilizaliturri-Flores I ( a Laboratorio de Investigación Bioquímica, Doctorado en Ciencias en Biotecnología , ENMH, Instituto Politécnico Nacional , Guillermo Massieu Helguera #239 Fracc. 'La Escalera' Ticoman, C.P. 07320, D.F. México , Mexico .)
Abstract	The anti-apoptotic B-cell lymphoma 2 (Bcl-2) protein interacts with several proteins that regulate the apoptotic properties of cells. In this research, we conduct several all-atom molecular dynamics (MD) simulations under high-temperature unfolding conditions, from 400 to 800 K, for 25 ns. These simulations were performed using a model of an engineered Bcl-2 human protein (Bcl-2-Δ22Σ3), which lacks 22 C-terminal residues of the transmembrane domain. The aim of this study is to gain insight into the structural behavior of Bcl-2-Δ22Σ3 by mapping the conformational movements involved in Bcl-2 stability and its biological function. To build a Bcl-2-Δ22Σ3 three-dimensional model, the protein core was built by homology modeling and the flexible loop domain (FLD, residues 33-91) by ab initio methods. Further, the entire protein model was refined by MD simulations. Afterwards, the production MD simulations showed that the FLD at 400 and 500 K has several conformations reaching into the protein core, whereas at 600 K some of the alpha-helices were lost. At 800 K, the Bcl-2 core is destabilized suggesting a possible mechanism for protein unfolding, where the alpha helices 1 and 6 were the most stable, and a reduction in the number of hydrogen bonds initially occurs. In conclusion, the structural changes and the internal protein interactions suggest that the core and the FLD are crucial components of Bcl-2 in its function of regulate ng access to the recognition sites of kinases and caspases.
File Format	HTM / HTML
ISSN	07391102
Issue Number	11
Volume Number	32
e-ISSN	15380254
Journal	Journal of Biomolecular Structure and Dynamics
Language	English
Publisher	Taylor & Francis
Publisher Date	2014-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Proto-oncogene Proteins C-bcl-2 Chemistry Amino Acid Sequence Hot Temperature Humans Hydrogen Bonding Molecular Dynamics Simulation Molecular Sequence Data Protein Conformation Protein Denaturation Protein Stability Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Medicine Molecular Biology

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