3ILC
Crystal structure of mouse Bcl-xl mutant (Y101A) at pH 6.0
Summary for 3ILC
| Entry DOI | 10.2210/pdb3ilc/pdb |
| Related | 3IHC 3IHD 3IHE 3IHF 3IIG 3IIH 3ILB |
| Descriptor | Bcl-2-like protein 1 (2 entities in total) |
| Functional Keywords | apoptosis, bh3 domain, bcl-2, alternative splicing, cytoplasm, membrane, mitochondrion, transmembrane |
| Biological source | Mus musculus (mouse) |
| Cellular location | Isoform Bcl-X(L): Mitochondrion membrane. Isoform Bcl-X(delta-TM): Cytoplasm: Q64373 |
| Total number of polymer chains | 1 |
| Total formula weight | 22102.26 |
| Authors | Priyadarshi, A.,Hwang, K.Y. (deposition date: 2009-08-07, release date: 2010-04-14, Last modification date: 2023-11-01) |
| Primary citation | Priyadarshi, A.,Roy, A.,Kim, K.S.,Kim, E.E.,Hwang, K.Y. Structural insights into mouse anti-apoptotic Bcl-xl reveal affinity for Beclin 1 and gossypol. Biochem.Biophys.Res.Commun., 2010 Cited by PubMed Abstract: This study reports the crystal structures of Bcl-xl wild type and three Bcl-xl mutants (Y101A, F105A, and R139A) with amino acid substitutions in the hydrophobic groove of the Bcl-xl BH3 domain. An additional 12 ordered residues were observed in a highly flexible loop between the alpha1 and alpha2 helices, and were recognized as an important deamidation site for the regulation of apoptosis. The autophagy-effector protein, Beclin 1, contains a novel BH3 domain (residues 101-125), which binds to the surface cleft of Bcl-xl, as confirmed by nuclear magnetic resonance (NMR) spectroscopy and analytical gel-filtration results. Gossypol, a potent inhibitor of Bcl-xl, had a K(d) value of 0.9 microM. In addition, the structural and biochemical analysis of five Bcl-xl substitution mutants will provide structural insights into the design and development of anti-cancer drugs. PubMed: 20206602DOI: 10.1016/j.bbrc.2010.03.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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