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TitlePUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis.
Journal, issue, pagesNat. Chem. Biol., Vol. 9, Page 163-168, Year 2013
Publish dateOct 19, 2012 (structure data deposition date)
AuthorsFollis, A.V. / Chipuk, J.E. / Fisher, J.C. / Yun, M.K. / Grace, C.R. / Nourse, A. / Baran, K. / Ou, L. / Min, L. / White, S.W. ...Follis, A.V. / Chipuk, J.E. / Fisher, J.C. / Yun, M.K. / Grace, C.R. / Nourse, A. / Baran, K. / Ou, L. / Min, L. / White, S.W. / Green, D.R. / Kriwacki, R.W.
External linksNat. Chem. Biol. / PubMed:23340338
MethodsNMR (solution) / X-ray diffraction
Resolution2.9 Å
Structure data

PDB-2m03:
Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains
Method: SOLUTION NMR

PDB-2m04:
Solution structure of BCL-xL in complex with PUMA BH3 peptide
Method: SOLUTION NMR

PDB-4hnj:
Crystallographic structure of BCL-xL domain-swapped dimer in complex with PUMA BH3 peptide at 2.9A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsAPOPTOSIS / BCL-xL / PUMA / Apoptosis/PROTEIN BINDING / Apoptosis-PROTEIN BINDING complex / BCL2-family / domain-swapped dimer / apoptosis regulation

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