Bh3 induced conformational changes in Bcl‐Xl revealed by crystal structure and comparative analysis
作者： Sreekanth Rajan , Minjoo Choi , Kwanghee Baek , Ho Sup Yoon
DOI: 10.1002/PROT.24816
关键词: Cell biology 、 Bacterial outer membrane 、 Bcl-xL 、 Apoptosis 、 Sequence (biology) 、 Alpha (ethology) 、 Biology 、 Programmed cell death 、 Cell 、 Mitochondrion
摘要: Apoptosis or programmed cell death is a regulatory process in cells response to stimuli perturbing physiological conditions. The Bcl-2 family of proteins plays an important role regulating homeostasis during apoptosis. In the process, molecular interactions among three members this family, pro-apoptotic, anti-apoptotic and BH3-only at mitochondrial outer membrane define fate cell. Here, we report crystal structures human protein Bcl-XL complex with BID(BH3) BIM(BH3) peptides determined 2.0 A 1.5 resolution, respectively. BH3 bind canonical hydrophobic pocket adopt alpha helical conformation bound form. Despite similar structural fold, comparison other complexes revealed differences due their sequence variations. Bcl-XL-BID(BH3) observed large pocket, complexes, lined by residues from helices α1, α2, α3, α5 located adjacent pocket. These results suggest that there are mode may translate into functional apoptotic regulation.
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