期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 356, 期 2, 页码 367-381出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2005.11.032
关键词
3D-domain swapping; apoptosis; BCL-X-L; dimer; X-ray crystallography
资金
- NCI NIH HHS [U01 CA91310, T32CA080416, U01 CA091310-04, U01 CA091310] Funding Source: Medline
Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 protein family are dynamically regulated and intimately involved in survival and death functions. We report the structure of a BCL-X-L homodimers a 3D-domain swapped dimer (3DDS). The X-ray crystal structure demonstrates the mutual exchange of carboxy-terminal regions including BH2 (Bcl-2 homology 2) between monomer subunits, with the hinge region occurring at the hairpin turn between the fifth and sixth alpha helices. Both BH3 peptide-binding hydrophobic grooves are unoccupied in the 3DDS dimer and available for BH3 peptide binding, as confirmed by sedimentation velocity analysis. BCL-X-L 3DDS dimers have increased pore-forming activity compared to monomers, suggesting that 3DDS dimers. may act as intermediates in membrane pore formation. Chemical crosslinking studies of Cys-substituted BCL-X-L proteins demonstrate that 3DDS dimers form in synthetic lipid vesicles. (c) 2005 Elsevier Ltd. All rights reserved.
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