1F16: SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX - RCSB PDB
2000年5月18日 · The solution structure of Bax, including the putative transmembrane domain at the C terminus, was determined in order to understand the regulation of its subcellular location. Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor, Bcl-x(L).
2K7W: BAX Activation is Initiated at a Novel Interaction Site - RCSB PDB
2008年8月27日 · BAX is a pro-apoptotic protein of the BCL-2 family that is stationed in the cytosol until activated by a diversity of stress stimuli to induce cell death. Anti-apoptotic proteins such as BCL-2 counteract BAX-mediated cell death.
RCSB PDB - 6EB6: Crystal structure of BAX W139A monomer
2018年8月5日 · BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association. To elicit apoptosis, BAX metamorphoses from an inert cytosolic monomer into homo-oligomers that permeabilize the mitochondrial outer membrane (MOM).
Allosteric sensitization of proapoptotic BAX - Nature
2017年7月10日 · BCL-2-associated X protein (BAX) is a critical apoptotic regulator that can be transformed from a cytosolic monomer into a lethal mitochondrial oligomer, yet drug...
1F16: SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
Download Stucture Data? 192 residues, click to see VAST similar structures. * Click molecule labels to explore molecular sequence information. Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. " MMDB and VAST+: tracking structural similarities between macromolecular complexes.
RCSB PDB - 5W63: Crystal structure of channel catfish BAX
2017年6月16日 · BAX and BAK are essential mediators of intrinsic apoptosis that permeabilize the mitochondrial outer membrane. BAX activation requires its translocation from cytosol to mitochondria where conformational changes cause its oligomerization.
PDB Entry - 1F16 - Protein Data Bank
2000年5月18日 · PDB Entry - 1F16 (Status - Released) Summary information: Title: SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX. PDB DOI: https://doi.org/10.2210/pdb1f16/pdb. Primary publication DOI: https://doi.org/10.1016/S0092-8674(00)00167-7. Entry authors: Suzuki, M., Youle, R.J., Tjandra, N. Initial deposition on: 18 May 2000. Initial release on: 22 ...
Small-molecule allosteric inhibitors of BAX - Nature
2019年2月4日 · Here, we describe a class of small-molecule BAX inhibitors, termed BAIs, that bind directly to a previously unrecognized pocket and allosterically inhibit BAX activation. BAI binding around the...
Physiological and pharmacological modulation of BAX - PubMed
Bcl-2-associated X protein (BAX) is a critical executioner of mitochondrial regulated cell death through its lethal activity of permeabilizing the mitochondrial outer membrane (MOM). While the physiological function of BAX ensures tissue homeostasis, dysregulation of BAX leads to …
RCSB PDB - 4S0O: Crystal Structure of the Autoinhibited Dimer of …
2015年1月2日 · Following a pro-apoptotic trigger, cytosolic BAX is activated and translocates to the mitochondria to initiate mitochondrial dysfunction and apoptosis. Here, cellular, biochemical, and structural data unexpectedly demonstrate that cytosolic BAX also has an inactive dimer conformation that regulates its activation.