1BXL

STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1BXL

• Entry DOI: 10.2210/pdb1bxl/pdb
• Descriptor: BCL-XL, BAK PEPTIDE (2 entities in total)
• Functional Keywords: apoptosis, alternative splicing, complex (apoptosis-peptide), complex (apoptosis-peptide) complex, complex (apoptosis/peptide)
• Biological source: Escherichia coli
• Cellular location: Mitochondrion membrane; Single-pass membrane protein (By similarity): Q07817; Mitochondrion membrane; Single-pass membrane protein (Potential): Q16611
• Total number of polymer chains: 2
• Total formula weight: 26606.31

Authors

Sattler, M.,Liang, H.,Nettesheim, D.,Meadows, R.P.,Harlan, J.E.,Eberstadt, M.,Yoon, H.,Shuker, S.B.,Chang, B.S.,Minn, A.J.,Thompson, C.B.,Fesik, S.W. (deposition date: 1996-10-16, release date: 1997-10-29, Last modification date: 2024-05-22)

Primary citation

Sattler, M.,Liang, H.,Nettesheim, D.,Meadows, R.P.,Harlan, J.E.,Eberstadt, M.,Yoon, H.S.,Shuker, S.B.,Chang, B.S.,Minn, A.J.,Thompson, C.B.,Fesik, S.W.
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
Science, 275:983-986, 1997

PubMed Abstract: Heterodimerization between members of the Bcl-2 family of proteins is a key event in the regulation of programmed cell death. The molecular basis for heterodimer formation was investigated by determination of the solution structure of a complex between the survival protein Bcl-xL and the death-promoting region of the Bcl-2-related protein Bak. The structure and binding affinities of mutant Bak peptides indicate that the Bak peptide adopts an amphipathic alpha helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions. Mutations in full-length Bak that disrupt either type of interaction inhibit the ability of Bak to heterodimerize with Bcl-xL.

PubMed: 9020082
DOI: 10.1126/science.275.5302.983

Experimental method

SOLUTION NMR