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Anti‐apoptotic Bcl‐X~L~ protein in complex with BH3 peptides of pro‐apoptotic Bak, Bad, and Bim proteins: Comparative molecular dynamics simulations by Dilraj Lama; Ramasubbu Sankararamakrishnan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The Bcl‐2 family of proteins plays a central role in the regulation of mitochondrial outer‐membrane permeabilization, a critical step in apoptosis. Heterodimerization between the pro‐ and anti‐apoptotic members of Bcl‐2 family is a key event in this process. Anti‐apoptotic proteins have high levels of expression in many cancers and they have different affinities for different pro‐apoptotic proteins. Experimentally determined structures of all members of Bcl‐2 proteins have remarkably similar helical fold despite poor amino acid sequence identity. Peptides representing BH3 region of pro‐apoptotic proteins have been shown to bind the hydrophobic cleft of anti‐apoptotic proteins and this segment is responsible in modulating the apoptotic pathways in living cells. Understanding the molecular basis of protein–protein recognition is required to develop inhibitors specific to a particular anti‐apoptotic protein. We have carried out molecular dynamics simulations on the anti‐apoptotic Bcl‐X~L~ protein in complex with three different BH3 peptides derived from pro‐apoptotic Bak, Bad and Bim proteins. Each complex structure was simulated for a period of 50 ns after 2.5 ns equilibr

Who reads Anti‐apoptotic Bcl‐X~L~ protein in complex with BH3 peptides of pro‐apoptotic Bak, Bad, and Bim proteins: Comparative molecular dynamics simulations?

Author

Dilraj Lama; Ramasubbu Sankararamakrishnan

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)