1AF3
RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN
Summary for 1AF3
| Entry DOI | 10.2210/pdb1af3/pdb |
| Descriptor | APOPTOSIS REGULATOR BCL-X (2 entities in total) |
| Functional Keywords | bcl-xl, apoptosis, mitochondrion, alternative splicing, regulatory protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Isoform Bcl-X(L): Mitochondrion inner membrane: P53563 |
| Total number of polymer chains | 1 |
| Total formula weight | 22082.25 |
| Authors | Aritomi, M.,Kunishima, N.,Inohara, N.,Ishibashi, Y.,Ohta, S.,Morikawa, K. (deposition date: 1997-03-21, release date: 1997-07-07, Last modification date: 2024-02-07) |
| Primary citation | Aritomi, M.,Kunishima, N.,Inohara, N.,Ishibashi, Y.,Ohta, S.,Morikawa, K. Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family. J.Biol.Chem., 272:27886-27892, 1997 Cited by PubMed Abstract: Bcl-xL is a member of the Bcl-2 protein family, which regulates apoptosis. Preparation of recombinant rat Bcl-xL yielded two forms, one deamidated at -Asn-Gly- sequences to produce isoaspartates and the other not deamidated. The crystal structures of the two forms show that they both adopt an essentially identical backbone structure which resembles the fold of human Bcl-xL: three layers of two alpha-helices each, capped at one end by two short helices. Both forms have a long disordered region, which contains the potential deamidation sites. The molecular structure exhibits a low level of interhelical interactions, the presence of three cavities, and a notable hydrophobic cleft surrounded by walls rich in basic residues. These unique structural features may be favorable for its accommodation into membranes or for possible rearrangement to modulate homo-/heterodimerization. Homology modeling of Bcl-2 and Bax, based on the Bcl-xL structure, suggests that Bax has the strongest potential for membrane insertion. Furthermore, we found a possible interface for interaction with non-Bcl-2 family member proteins, such as CED-4 homologues. PubMed: 9346936DOI: 10.1074/jbc.272.44.27886 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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