![]() ![]() Received: ApAccepted: AugPublished: September 18, 2015Ĭopyright: © 2015 Cabral et al. PLoS ONE 10(9):Įditor: Israel Silman, Weizmann Institute of Science, ISRAEL (2015) Biophysical Studies on BEX3, the p75 NTR-Associated Cell Death Executor, Reveal a High-Order Oligomer with Partially Folded Regions. The self-oligomerization of BEX3 has been previously reported in cell culture and is consistent with our in vitro data.Ĭitation: Cabral KMS, Raymundo DP, Silva VS, Sampaio LAG, Johanson L, Hill LF, et al. Solution nuclear magnetic resonance, partial proteinase K digestion, circular dichroism spectroscopy, and fluorescence techniques that were performed on the recombinant protein indicated that the structure of BEX3 is composed of approximately 31% α-helix and 20% β-strand, contains partially folded regions near the N- and C-termini, and a core which is proteolysis-resistant around residues 55–120. Small angle X-ray scattering and atomic force microscopy revealed that BEX3 forms a specific higher-order oligomer that is consistent with a globular molecule. In this study, we structurally characterized BEX3 using biophysical experimental data. The pro-apoptotic activity of BEX3 in association with a number of additional proteins has been widely supported however, to the best of our knowledge, very limited data are available on the conformation of any of the members of the BEX family. BEX3 has been predicted to be intrinsically disordered and also to represent an intracellular hub for cell signaling. ![]() Several studies have found the BEX proteins to be associated with neurodegeneration, the cell cycle and cancer. BEX3 (Brain Expressed X–linked protein 3) is a member of a mammal-specific placental protein family.
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