Structural insights into mouse anti-apoptotic Bcl-xl reveal affinity for Beclin 1 and gossypol
- Authors
- Priyadarshi, Amit; Roy, Ankoor; Kim, Key Sun; Kim, Eunice EunKyeong; Hwang, Kwang Yeon
- Issue Date
- 9-4월-2010
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Bcl-xl; Beclin; Apoptosis; Gossypol; Mutation
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.394, no.3, pp.515 - 521
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 394
- Number
- 3
- Start Page
- 515
- End Page
- 521
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/116637
- DOI
- 10.1016/j.bbrc.2010.03.002
- ISSN
- 0006-291X
- Abstract
- This study reports the crystal structures of Bcl-xl wild type and three Bcl-xl mutants (Y101A, F105A, and R139A) with amino acid substitutions in the hydrophobic groove of the Bcl-xl BH3 domain An additional 12 ordered residues were observed in a highly flexible loop between the alpha 1 and alpha 2 helices, and were recognized as an important deamidation site for the regulation of apoptosis The autophagy-effector protein, Beclin 1, contains a novel BH3 domain (residues 101-125), which binds to the surface cleft of Bcl-xl, as confirmed by nuclear magnetic resonance (NMR) spectroscopy and analytical gel-filtration results Gossypol, a potent inhibitor of Bcl-xl, had a K-d value of 0 9 mu M In addition, the structural and biochemical analysis of five Bcl-xl substitution mutants will provide structural insights into the design and development of anti-cancer drugs (C) 2010 Elsevier Inc All rights reserved
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.