Structure of Bcl-x(L)-Bak peptide complex: Recognition between regulators of apoptosis

Science

Volumn 275, Issue 5302, 1997, Pages 983-986

  Sattler, Michael ^a   Liang, Heng ^a   Nettesheim, David ^a   Meadows, Robert P ^a   Harlan, John E ^a   Eberstadt, Matthias ^a   Yoon, Ho Sup ^a   Shuker, Suzanne B ^a   Chang, Brian S ^b   Minn, Andy J ^b   Thompson, Craig B ^b   Fesik, Stephen W ^a  

^a ABBOTT LABORATORIES   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN BCL 2; MEMBRANE PROTEIN; ONCOPROTEIN; PROTEIN BAK; PROTEIN BCL X;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CELL DEATH; COMPLEX FORMATION; DIMERIZATION; ELECTRICITY; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; APOPTOSIS; CHEMICAL STRUCTURE; CHEMISTRY; GENE DELETION; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; APOPTOSIS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; BCL-X PROTEIN; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2; SEQUENCE DELETION;

EID: 0030614915     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5302.983     Document Type: Article

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14. L as a function of increasing peptide concentration. The excitation and emission wavelengths were 290 and 340 nm, respectively.
15. 2O.
16. 2O. The recombinant protein was purified by affinity chromatography on a nickel-IDA column (Invitrogen) followed by ion-exchange chromatography on an S-Sepharose column.
17. -1.
18. -1.
19. -1.
20. -1.
21. -1.
22. -1.
23. L is reduced to a single helical turn, and residues 198 to 205 form an additional helix.
24. M. Eberstadt, M. Sattler, S. W. Fesik, unpublished data.
25. B. Chang, A. J. Minn, C. B. Thompson, unpublished data.
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27. L-Bak peptide complex have been deposited in the Brookhaven Protein Data Bank (accession number 1BXL).