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Structure paper

TitleEpistatic mutations in PUMA BH3 drive an alternate binding mode to potently and selectively inhibit anti-apoptotic Bfl-1.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateFeb 17, 2017 (structure data deposition date)
AuthorsJenson, J.M. / Ryan, J.A. / Grant, R.A. / Letai, A. / Keating, A.E.
External linksElife / PubMed:28594323
MethodsX-ray diffraction
Resolution1.199 - 2.346 Å
Structure data

PDB-5uuk:
Human Bfl-1 in complex with a Bfl-1-specific selected peptide
Method: X-RAY DIFFRACTION / Resolution: 1.199 Å

PDB-5uul:
Human Bfl-1 in complex with PUMA BH3
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

PDB-5uum:
Human Mcl-1 in complex with a Bfl-1-specific selected peptide
Method: X-RAY DIFFRACTION / Resolution: 2.346 Å

PDB-5uup:
Human Bfl-1 covalently cross-linked to an electrophilic variant of a Bfl-1-specific selected peptide
Method: X-RAY DIFFRACTION / Resolution: 1.726 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsAPOPTOSIS / Apoptosis Regulatory Proteins / Peptide Library / Protein Binding / Protein Structure / Proto-Oncogene / Specificity / BCL2A1 / BCL2 related protein A1 / Peptide Inhibitor / Electrophile

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