4HNJ
Crystallographic structure of BCL-xL domain-swapped dimer in complex with PUMA BH3 peptide at 2.9A resolution
Summary for 4HNJ
Entry DOI | 10.2210/pdb4hnj/pdb |
Related | 2M03 2M04 |
Descriptor | Bcl-2-like protein 1, Bcl-2-binding component 3 (3 entities in total) |
Functional Keywords | bcl2-family, domain-swapped dimer, apoptosis regulation, bcl-xl, puma, apoptosis-protein binding complex, apoptosis/protein binding |
Biological source | Homo sapiens (human) More |
Cellular location | Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817 Mitochondrion : Q9BXH1 |
Total number of polymer chains | 3 |
Total formula weight | 50393.22 |
Authors | Fisher, J.C.,Yun, M.K.,White, S.W. (deposition date: 2012-10-19, release date: 2013-01-23, Last modification date: 2023-09-20) |
Primary citation | 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. PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. Nat.Chem.Biol., 9:163-168, 2013 Cited by PubMed: 23340338DOI: 10.1038/nchembio.1166 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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