mirage

Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations

DSpace/Manakin Repository

 

Search DR-NTU


Advanced Search Subject Search

Browse

My Account

Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations

Show simple item record

dc.contributor.author Bharatham, Nagakumar
dc.contributor.author Chi, Seung-Wook
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-02-07T03:28:51Z
dc.date.available 2012-02-07T03:28:51Z
dc.date.copyright 2011
dc.date.issued 2012-02-07
dc.identifier.citation Bharatham, N., Chi S. W., Yoon, H. S. (2011). Molecular Basis of Bcl-XL-p53 Interaction: Insights from Molecular Dynamics Simulations. PLoS ONE, 6(10), 1-12.
dc.identifier.uri http://hdl.handle.net/10220/7512
dc.description.abstract Bcl-XL, an antiapoptotic Bcl-2 family protein, plays a central role in the regulation of the apoptotic pathway. Heterodimerization of the antiapoptotic Bcl-2 family proteins with the proapoptotic family members such as Bad, Bak, Bim and Bid is a crucial step in the apoptotic regulation. In addition to these conventional binding partners, recent evidences reveal that the Bcl-2 family proteins also interact with noncanonical binding partners such as p53. Our previous NMR studies showed that Bcl-XL: BH3 peptide and Bcl-XL: SN15 peptide (a peptide derived from residues S15-N29 of p53) complex structures share similar modes of bindings. To further elucidate the molecular basis of the interactions, here we have employed molecular dynamics simulations coupled with MM/PBSA approach. Bcl-XL and other Bcl-2 family proteins have 4 hydrophobic pockets (p1–p4), which are occupied by four systematically spaced hydrophobic residues (h1–h4) of the proapoptotic Bad and Bak BH3 peptides. We observed that three conserved hydrophobic residues (F19, W23 and L26) of p53 (SN15) peptide anchor into three hydrophobic pockets (p2–p4) of Bcl-XL in a similar manner as BH3 peptide. Our results provide insights into the novel molecular recognition by Bcl-XL with p53.
dc.format.extent 12 p.
dc.language.iso en
dc.relation.ispartofseries PLoS one
dc.rights © 2011 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.subject DRNTU::Science::Biological sciences
dc.title Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1371/journal.pone.0026014
dc.description.version Published version

Files in this item

Files Size Format View
journal.pone.0026014.pdf 656.7Kb PDF View/Open

This item appears in the following Collection(s)

Show simple item record

Statistics

Total views

All Items Views
Molecular basis of Bcl-XL-p53 interaction : insights from molecular dynamics simulations 298

Total downloads

All Bitstreams Views
journal.pone.0026014.pdf 191

Top country downloads

Country Code Views
China 67
United States of America 55
Singapore 25
Taiwan 15
Germany 2

Top city downloads

city Views
Beijing 52
Mountain View 44
Singapore 24
Tainan 10
Shanghai 3

Downloads / month

  2014-06 2014-07 2014-08 total
journal.pone.0026014.pdf 0 0 7 7