Proteopedia - User contributions [en]

User:Chloe Tucker/Sandbox 1

2024-04-26T20:42:59Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR (light blue) and GIP (dark blue) residue interactions]]
The <scene name='10/1038815/Overview/7'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. '''Figure 1''' shows many of the interactions between GIP and GIPR. All of these interactions are responsible for the binding affinity, the strength of the attraction, between the two proteins. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. GIPR (pink) and Tirzepatide (dark pink) residue interactions]]
The <scene name='10/1038815/Tirzepatide_active_site/4'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain and activating cellular signaling.The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. '''Figure 2''' shows the interactions between GIPR and Tirzepatide, along with the slight changes in conformation and hydrogen bonding. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. The more hydrogen bonding there is between molecules, the stronger the binding between the two molecules will be. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/3'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-26T20:35:36Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR (light blue) and GIP (dark blue) residue interactions]]
The <scene name='10/1038815/Overview/7'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. '''Figure 1''' shows many of the interactions between GIP and GIPR. All of these interactions are responsible for the binding affinity, the strength of the attraction, between the two proteins. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. GIPR (pink) and Tirzepatide (dark pink) residue interactions]]
The <scene name='10/1038815/Tirzepatide_active_site/4'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain and activating cellular signaling.The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. '''Figure 2''' shows the interactions between GIPR and Tirzepatide, along with the slight changes in conformation and hydrogen bonding. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. The more hydrogen bonding there is between molecules, the stronger the binding between the two molecules will be. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/2'>I7</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>T7</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-26T20:34:08Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/7'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. '''Figure 1''' shows many of the interactions between GIP and GIPR. All of these interactions are responsible for the binding affinity, the strength of the attraction, between the two proteins. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/4'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain and activating cellular signaling.The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. '''Figure 2''' shows the interactions between GIPR and Tirzepatide, along with the slight changes in conformation and hydrogen bonding. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. The more hydrogen bonding there is between molecules, the stronger the binding between the two molecules will be. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/2'>I7</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>T7</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-26T20:26:12Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/7'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/4'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/2'>I7</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>T7</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-26T20:21:53Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/6'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/N-term_of_gip/25'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/2'>I7</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>T7</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-26T20:06:01Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/N-term_of_gip/25'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/2'>I7</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/3'>T7</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:46:00Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/N-term_of_gip/25'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/7'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:22:32Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/N-term_of_gip/25'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:18:49Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/3'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:12:36Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. Threonine 7 (T7) is also making a hydrogen bone with the Arginine 190 (R190) residue. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:10:46Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:09:59Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>binding site</scene> with Tirzepatide is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they are now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:09:12Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they are now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:08:54Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they are now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue <scene name='10/1038815/Tirzepatide_thr7/2'>(T7)</scene>. Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.
<scene name='10/1038815/Tirzepatide_thr7/2'>Threonine 7</scene>

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:08:05Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they are now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
In GIP there is an Isoleucine present <scene name='10/1038815/Gip_ile7/1'>(I7)</scene>. Isoleucine is a branched residue that is very hydrophobic. This residue is also present in the N-term where the important interactions are occuring. In Tirzepatide, this seventh residue has been changed to a Threonine residue (T7). Threonine is also a branched residue, but it contains a hydroxyl group making it hydrophilic, allowing it to make hydrogen bonds. This extra hydrogen bond in Tirzepatide is also responsible for a higher binding affinity for the drug than GIP itself.
<scene name='10/1038815/Tirzepatide_thr7/2'>Threonine 7</scene>

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:01:18Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide, the most noticeable conformational change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they are now form a new hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
<scene name='10/1038815/Tirzepatide_thr7/2'>Threonine 7</scene>
<scene name='10/1038815/Gip_ile7/1'>Isoleucine 7</scene>

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T14:00:33Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins will be. In Tirzepatide the most noticeable change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
<scene name='10/1038815/Tirzepatide_thr7/2'>Threonine 7</scene>
<scene name='10/1038815/Gip_ile7/1'>Isoleucine 7</scene>

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T13:59:43Z

Chloe Tucker:

=GIP and GIP-R=
<StructureSection load='7RA3' size='340' side='right' caption='GIP with GIP receptor' scene='10/1038815/Overview/1'>
This is a default text for your page '''Chloe Tucker/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.

== Introduction ==
[https://www.cdc.gov/diabetes/basics/diabetes.html#:~:text=With%20diabetes%2C%20your%20body%20doesn,vision%20loss%2C%20and%20kidney%20disease. Diabetes]
== Function ==
<ref name="Sun">PMID:35333651 </ref>.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
=== Binding/Active Site of GIPR with GIP ===
[[Image:GIP_hydrogen_bonds.jpg|350 px|right|thumb|Figure 1. GIPR and GIP residue interactions]]
The <scene name='10/1038815/Overview/3'>binding site</scene> of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell.
Many other <scene name='10/1038815/Active_site/3'>residues</scene> within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)<ref name="Sun"/>. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

=== Binding/Active Site of GIPR with Tirzepatide ===
[[Image:TZ_hydrogen_bonds.jpg|350 px|right|thumb|Figure 2. Residue Interactions with Tirzepatide]]
The <scene name='10/1038815/Tirzepatide_active_site/2'>Tirzepatide binding site</scene> is the same as GIP with the N-term binding to the transmembrane domain.
The <scene name='10/1038815/Tirzepatide_residues/5'>residues</scene> are fairly similar just in a different conformations, which is allowing for more hydrogen bonding. The more hydrogen bonding there is the stronger the binding between the two proteins is. In Tirzepatide the most noticeable change is the Tyrosine 1 (Y1) residue. It is now facing up towards Arginine 190 (R190) where they can now form a hydrogen bond that was not present in GIP. This can lead to the conclusion that GIPR has a higher binding affinity for Tirzepatide than GIP itself<ref name="Sun"/>.
=== Isoleucine vs. Threonine ===
<scene name='10/1038815/Tirzepatide_thr7/2'>Threonine 7</scene>
<scene name='10/1038815/Gip_ile7/1'>Isoleucine 7</scene>

</StructureSection>
== References ==
<ref name="Sun">PMID:35333651</ref>
== Student Contributors ==
*Chloe Tucker
*Mandy Bechman

User:Chloe Tucker/Sandbox 1

2024-04-25T13:51:12Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:47:44Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:46:43Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:41:27Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:40:14Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:38:58Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:38:04Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:34:11Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-25T13:18:53Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-24T20:12:18Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-18T14:27:08Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-18T14:24:30Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-11T14:37:01Z

Chloe Tucker:

File:GIP hydrogen bonds.jpg

2024-04-11T14:36:39Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-11T14:35:15Z

Chloe Tucker:

File:TZ hydrogen bonds.jpg

2024-04-11T14:33:32Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-11T14:18:04Z

Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

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Chloe Tucker:

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Chloe Tucker:

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Chloe Tucker:

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

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Chloe Tucker:

User:Chloe Tucker/Sandbox 1

2024-04-11T13:04:23Z

Chloe Tucker: