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. 2021 May 19;12:675708. doi: 10.3389/fphys.2021.675708

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Copyright © 2021 Di Rosa, Guarino, Conti Nibali, Magrì and De Pinto.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structural features of yeast voltage-dependent anion selective channel (VDAC) isoforms. (A) Multi-alignment analysis of the amino acid sequences of yVDAC1 and yVDAC2 (source: GeneBank). Colors highlight the conserved (orange) or similar (yellow) residues. (B) Lateral and top view of the superposition of yVDACs. The predicted structure of yVDAC1 (in brigthorange) and yVDAC2 (in teal) were obtained by homology modeling using MODELLER 9.24 software and the human VDAC1 structure (PDB ID: 2JK4) as template. Final figures were drawn using PyMol software.