Proteopedia - User contributions [en]

User:Victor Reverte/Sandbox 1

2019-06-10T13:16:24Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease<ref>DOI 10.1038/nrm1155</ref>. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival<ref>DOI 10.1038/nrm3412</ref>. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.<ref>DOI 10.7554/eLife.00704</ref>

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix<ref>DOI 10.1038/ncb2868</ref>. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex<ref>DOI 10.1161/CIRCRESAHA.116.305484</ref>.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''<ref>DOI 10.1016/j.chembiol.2016.07.012</ref>.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML)<ref>DOI 10.1016/j.cell.2019.03.050</ref>.

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang<ref>DOI 10.1016/j.cell.2019.03.050</ref>

== Disease ==

While having a crucial role in calcium homeostasis, mitochondrial calcium uptake was already reported as protective to neuron excitotoxicity<ref>DOI 10.1111/acel.12527</ref> and liver ischemia-reperfusion damage<ref>DOI 10.1016/j.freeradbiomed.2017.06.013</ref>. Therefore, mutations and dysfunction of '''MCU''' could aggravate these kinds of insult. Also, MCU could be protective to skeletal muscle age related atrophy, as suggested by it’s increase expression upon exercise stimuli<ref>DOI 10.14814/phy2.13005</ref>.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-10T13:13:18Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease<ref>DOI 10.1038/nrm1155</ref>. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival<ref>DOI 10.1038/nrm3412</ref>. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.<ref>DOI 10.7554/eLife.00704</ref>

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix<ref>DOI 10.1038/ncb2868</ref>. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex<ref>DOI 10.1161/CIRCRESAHA.116.305484</ref>.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''<ref>DOI 10.1016/j.chembiol.2016.07.012</ref>.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML)<ref>DOI 10.1016/j.cell.2019.03.050</ref>.

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang<ref>DOI 10.1016/j.cell.2019.03.050</ref>

== Disease ==

While having a crucial role in calcium homeostasis, mitochondrial calcium uptake was already reported as protective to neuron excitotoxicity and liver ischemia-reperfusion damage<ref>DOI 10.1111/acel.12527</ref>. Therefore, mutations and dysfunction of '''MCU''' could aggravate these kinds of insult. Also, MCU could be protective to skeletal muscle age related atrophy, as suggested by it’s increase expression upon exercise stimuli<ref>DOI 10.1016/j.freeradbiomed.2017.06.013</ref>.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T17:33:33Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease<ref>DOI 10.1038/nrm1155</ref>. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival<ref>DOI 10.1038/nrm3412</ref>. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.<ref>DOI 10.7554/eLife.00704</ref>

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang<ref>DOI 10.1016/j.cell.2019.03.050</ref>

== Disease ==

While having a crucial role in calcium homeostasis, mitochondrial calcium uptake was already reported as protective to neuron excitotoxicity and liver ischemia-reperfusion damage. Therefore, mutations and dysfunction of '''MCU''' could aggravate these kinds of insult. Also, MCU could be protective to skeletal muscle age related atrophy, as suggested by it’s increase expression upon exercise stimuli.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T17:26:57Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang<ref>DOI 10.1016/j.cell.2019.03.050</ref>

== Disease ==

While having a crucial role in calcium homeostasis, mitochondrial calcium uptake was already reported as protective to neuron excitotoxicity and liver ischemia-reperfusion damage. Therefore, mutations and dysfunction of '''MCU''' could aggravate these kinds of insult. Also, MCU could be protective to skeletal muscle age related atrophy, as suggested by it’s increase expression upon exercise stimuli.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T17:20:00Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang<ref>DOI 10.1016/j.cell.2019.03.050</ref>

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T17:08:50Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called '''MCU'''.

== Function ==

'''MCU''' is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled '''Mitochondrial Calcium Uniporter Complex (MCUC)''' along with '''EMRE''', '''MICU1''' and '''MICU2''', which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, '''MCU''' monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being '''N-terminal domain (NTD)''', '''linker helix domain (LHD)''', '''coiled-coil domain (CCD)''', and '''transmembrane domain (TMD)'''. '''CCD''' and '''TMD''' are the pore-forming subunits, while '''LHD''' links this regions to '''NTD'''. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of '''NTD'''.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T17:02:46Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

[[Image:Structure.png]]
This image is from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

File:Structure.png

2019-06-09T16:56:57Z

Victor Reverte: uploaded a new version of "Image:Structure.png": Image from the article "Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter" by Youxing Jiang and others.

User:Victor Reverte/Sandbox 1

2019-06-09T16:40:07Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by <scene name='81/817978/E264/2'>E264</scene> and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T16:20:00Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by E264 and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues <scene name='81/817978/E288_and_v290/1'>E288 and V290</scene> of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T16:07:45Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of <scene name='81/817978/D261/1'>D261 residues</scene> has a radius of affinity for hydrated calcium. The narrower one, is stabilized by E264 and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues E288 and V290 of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-09T15:55:36Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o5b' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, <scene name='81/817978/260wdimep265/1'>260WDIMEP265</scene>, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of D261 residues has a radius of affinity for hydrated calcium. The narrower one, is stabilized by E264 and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues E288 and V290 of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-08T18:56:08Z

Victor Reverte:

== Mitochondrial Calcium Uniporter (MCU) ==

<StructureSection load='6o58' size='340' side='right' caption='MCU (6O58)' scene=''>
Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, 260WDIMEP265, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of D261 residues has a radius of affinity for hydrated calcium. The narrower one, is stabilized by E264 and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues E288 and V290 of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Victor Reverte/Sandbox 1

2019-06-08T17:23:32Z

Victor Reverte: New page: == MCU == <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Victor Reverte/Sandbox 1'''. Click ab...

== MCU ==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Victor Reverte/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Ca+2 signalization in Mito ==

Calcium is a main signalling effector in eukaryotic cells. Therefore, its cellular concentration is tightly regulated through processes of calcium increase and decrease. Among decrease processes, mitochondria are organelles capable of buffering high concentrations of calcium, and by doing so, they become central on cellular signalling and survival. In humans, mitochondrial calcium uptake is mediated by a protein called MCU.

== Function ==

MCU is a highly selective uniporter that allows calcium entry into the mitochondrial matrix. In metazoa, it belongs to a protein complex entitled Mitochondrial Calcium Uniporter Complex (MCUC) along with EMRE, MICU1 and MICU2, which are respectively proposed as a regulator and gatekeepers of the complex.

== Structure ==

Being assembled as a tetramer, MCU monomers posses 351 amino acid residues. Each subunit can be divided into four structural domains, them being N-terminal domain (NTD), linker helix domain (LHD), coiled-coil domain (CCD), and transmembrane domain (TMD). CCD and TMD are the pore-forming subunits, while LHD links this regions to NTD. Recently, regulation of the complex and dimerization of two tetrameres were reported as functions of NTD.
To guarantee selectivity, 260WDIMEP265, a highly conserved sequence among protein homologues, from each monomer form two filters. The first one, dependent of D261 residues has a radius of affinity for hydrated calcium. The narrower one, is stabilized by E264 and its selective for calcium radius. Finally, there’s a second constriction point at the end of the pore, formed by residues E288 and V290 of each monomer, that are involved in a juxtamembrane loop (JML).

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>