https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Advika+Dhanorkar 2026-09-27T04:29:48Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396256 2025-11-30T10:34:22Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/3'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/2'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved &lt;scene name='10/1096829/Glycine_region/1'&gt;glycine-rich hinge&lt;/scene&gt; that may enable gating through helix repositioning. <br /> <br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396254 2025-11-30T10:31:51Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/2'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/2'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved &lt;scene name='10/1096829/Glycine_region/1'&gt;glycine-rich hinge&lt;/scene&gt; that may enable gating through helix repositioning. <br /> <br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396245 2025-11-30T10:27:34Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/2'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved &lt;scene name='10/1096829/Glycine_region/1'&gt;glycine-rich hinge&lt;/scene&gt; that may enable gating through helix repositioning. <br /> <br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396244 2025-11-30T10:26:28Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/2'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved &lt;scene name='10/1096829/Glycine_region/1'&gt;glycine-rich hinge&lt;/scene&gt; that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396233 2025-11-30T09:59:50Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/2'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396231 2025-11-30T09:58:23Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/Alpha_helix/1'&gt;N terminal alpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396222 2025-11-30T09:51:08Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved n terminal alpha helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396217 2025-11-30T09:47:18Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 and 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/N_terminal_alpha_helix/1'&gt;N-terminal αlpha helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396216 2025-11-30T09:45:09Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 an 19 are in a parallel orientation&lt;/scene&gt; to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved &lt;scene name='10/1096829/N_terminal_alpha_helix/1'&gt;N-terminal α-helix&lt;/scene&gt; positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396191 2025-11-30T09:04:35Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. &lt;scene name='10/1096829/Parallel_strands/1'&gt;Strands 1 an 19 are in a parallel orientation&lt;/scene&gt;to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396184 2025-11-30T08:17:05Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 (PDB ID- 3EMN) at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/Colours_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Vdac1_(3EMN):_BI3323-Aug2025&diff=4396180 2025-11-30T08:04:34Z

<p>Advika Dhanorkar: Vdac1 (3EMN): BI3323-Aug2025 moved to Mouse Vdac1: BI3323-Aug2025</p> <hr /> <div>#REDIRECT [[Mouse Vdac1: BI3323-Aug2025]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396179 2025-11-30T08:04:34Z

<p>Advika Dhanorkar: Vdac1 (3EMN): BI3323-Aug2025 moved to Mouse Vdac1: BI3323-Aug2025</p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_vdac&diff=4396178 2025-11-30T08:02:18Z

<p>Advika Dhanorkar: Mouse vdac moved to Vdac1 (3EMN): BI3323-Aug2025</p> <hr /> <div>#REDIRECT [[Vdac1 (3EMN): BI3323-Aug2025]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396177 2025-11-30T08:02:18Z

<p>Advika Dhanorkar: Mouse vdac moved to Vdac1 (3EMN): BI3323-Aug2025</p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396121 2025-11-30T06:04:16Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396119 2025-11-30T06:02:59Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396118 2025-11-30T06:02:38Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396116 2025-11-30T05:38:12Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a &lt;scene name='10/1096829/Terminals_group_colour/1'&gt;19 stranded β-barrel&lt;/scene&gt; - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396110 2025-11-30T05:21:12Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396108 2025-11-30T05:17:59Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/N_and_c_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a &lt;scene name='10/1096829/Secondary_structure/3'&gt;19 stranded β-barrel&lt;/scene&gt; - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396101 2025-11-30T05:01:10Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/N_and_c_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a &lt;scene name='10/1096829/Secondary_structure/1'&gt;19 stranded β-barrel &lt;/scene&gt; - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396096 2025-11-30T04:39:50Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> &lt;scene name='10/1096829/N_and_c_terminal/1'&gt;mVDAC1&lt;/scene&gt; forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4396088 2025-11-30T04:15:59Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å: BI3323-Aug2025==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395950 2025-11-29T15:40:29Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scene<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395949 2025-11-29T15:37:49Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Structure of mouse VDAC1 at 2.3 Å==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scen&lt;Structure load='3EMN' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;es.==Your Heading Here (maybe something like 'Structure')==<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395948 2025-11-29T15:37:13Z

<p>Advika Dhanorkar: </p> <hr /> <div>=='Structure of mouse VDAC1 at 2.3 Å')==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scen&lt;Structure load='3EMN' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;es.==Your Heading Here (maybe something like 'Structure')==<br /> <br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395947 2025-11-29T15:35:17Z

<p>Advika Dhanorkar: </p> <hr /> <div>=='Structure of mouse VDAC1 at 2.3 Å')==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scen&lt;Structure load='3EMN' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;es.==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='3emn' size='350' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395946 2025-11-29T15:24:47Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure of mouse VDAC1 at 2.3 Å')==<br /> &lt;StructureSection load='3EMN' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scen&lt;Structure load='3EMN' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;es.==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='3emn' size='350' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395945 2025-11-29T15:16:31Z

<p>Advika Dhanorkar: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure of mouse VDAC1 at 2.3 Å')==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='3emn' size='350' side='right' caption='Crystal structure of mouse VDAC1 (PDB entry [[3emn]])' scene=''&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]&lt;Structure load='3emn' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;'</div>

Advika Dhanorkar https://proteopedia.org/index.php?title=Mouse_Vdac1:_BI3323-Aug2025&diff=4395944 2025-11-29T15:10:49Z

<p>Advika Dhanorkar: New page: ==Your Heading Here (maybe something like &#039;Structure&#039;)== &lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&gt; This is a default text for you...</p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Mouse vdac'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Introduction ==<br /> The voltage dependent anion channel (VDAC) is the primary gateway for ions and metabolites crossing the mitochondrial outer membrane. It mediates the exchange of ATP and ADP and other essential metabolites contributing to mitochondrial physiology and apoptosis regulation. The properties of VDAC like voltage gating, ion selectivity shifts and interaction with modulatory proteins have been established previously. Earlier predictions varied widely on the number of β-strands in its barrel and the orientation of the voltage sensing N terminal remained unresolved. The resolution of the murine VDAC1 at 2.3 Å crystallized in lipidic bicelles gave mechanistic insights into gating and metabolite conductance.<br /> <br /> == Significance ==<br /> VDAC sits at the intersection of metabolism and apoptosis and its dysfunction contributes to diseases including cardiovascular disorders and cancer. High resolution structure enables to understand how VDAC regulates mitochondrial permeability and how metabolites and proteins modulate its activity. Precise structural knowledge enables rational drug design aimed at targeting VDAC mediated cell death pathways. Because VDAC interacts with other proteins such has hexokinase and Bcl-2 family members insights into its gating mechanism hold implications for therapeutic control of mitochondrial integrity and metabolic signaling.<br /> <br /> == Structural highlights ==<br /> mVDAC1 forms a 19 stranded β-barrel - the first high resolution eukaryotic β-barrel with an odd number of strands. Strands 1 an 19 are in a parallel orientation to close the barrel while the rest are antiparallel. The pore is wide, elliptical and hydrophilic consistent with the open state. A key finding is the well resolved N-terminal α-helix positioned against the barrel's interior wall, partially narrowing the pore and contributing positive charges that shape anion selectivity. The helix is tethered to the wall by multiple hydrogen bonds and connected through a conserved glycine-rich hinge that may enable gating through helix repositioning. <br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang, L. Toro, P. Ping, &amp; J. Abramson, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc. Natl. Acad. Sci. U.S.A. 105 (46) 17742-17747, https://doi.org/10.1073/pnas.0809634105 (2008).<br /> &lt;references/&gt;[[Link title]]&lt;Structure load='3EMN' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Advika Dhanorkar