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1BXL

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

Summary for 1BXL
Entry DOI10.2210/pdb1bxl/pdb
DescriptorBCL-XL, BAK PEPTIDE (2 entities in total)
Functional Keywordsapoptosis, alternative splicing, complex (apoptosis-peptide), complex (apoptosis-peptide) complex, complex (apoptosis/peptide)
Biological sourceEscherichia coli
Cellular locationMitochondrion membrane; Single-pass membrane protein (By similarity): Q07817
Mitochondrion membrane; Single-pass membrane protein (Potential): Q16611
Total number of polymer chains2
Total formula weight26606.31
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: 2022-02-16)
Primary citationSattler, 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
Cited by
PubMed: 9020082
DOI: 10.1126/science.275.5302.983
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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