A conserved hydrophobic core at Bcl-xL mediates its structural stability and binding affinity with BH3-domain peptide of pro-apoptotic protein

Archives of Biochemistry and Biophysics

Volumn 484, Issue 1, 2009, Pages 46-54

  Feng, Yu ^a   Zhang, Liang ^a   Hu, Tianchen ^a   Shen, Xu ^a,b   Ding, Jianping ^c   Chen, Kaixian ^a   Jiang, Hualiang ^a,b   Liu, Dongxiang ^a  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^c INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Bcl xL; Heterodimerization; Hydrophobic core; Pore formation; Protein stability

Indexed keywords

BH3 PROTEIN; PROTEIN BCL XL; TRYPTOPHAN;

APOPTOSIS; ARTICLE; BINDING AFFINITY; CORRELATION ANALYSIS; HYDROPHOBICITY; LIPID VESICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM;

AMINO ACID SEQUENCE; APOPTOSIS; BCL-X PROTEIN; CIRCULAR DICHROISM; CONSERVED SEQUENCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 62349106198     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.01.003     Document Type: Article

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