https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Emily+BerkmanProteopedia - User contributions [en]2026-09-28T13:33:28ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4130984Emily Berkman/Sandbox 22024-04-23T19:53:17Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<scene name='10/1037520/Y37_and_e74_ramp3/2'>TextToBeDisplayed</scene><br />
<scene name='10/1037516/R18/4'>TextToBeDisplayed</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species. <ref name="Bower">PMID:27061187</ref>]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/5'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species. This disulfide causes the N-terminus of amylin to wrap around. <ref name="Bower">PMID:27061187</ref><br />
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==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
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<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4130983Emily Berkman/Sandbox 22024-04-23T19:52:24Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<scene name='10/1037520/Y37_and_e74_ramp3/2'>TextToBeDisplayed</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species. <ref name="Bower">PMID:27061187</ref>]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/5'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species. This disulfide causes the N-terminus of amylin to wrap around. <ref name="Bower">PMID:27061187</ref><br />
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==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
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<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126928Emily Berkman/Sandbox 22024-04-16T19:53:58Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species. <ref name="Bower">PMID:27061187</ref>]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/5'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species. This disulfide causes the N-terminus of amylin to wrap around. <ref name="Bower">PMID:27061187</ref><br />
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==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126924Emily Berkman/Sandbox 22024-04-16T19:44:14Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species. <ref name="Bower">PMID:27061187</ref>]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/5'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
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==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126919Emily Berkman/Sandbox 22024-04-16T19:39:32Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/5'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
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==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126914Emily Berkman/Sandbox 22024-04-16T19:31:35Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/2'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
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<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126912Emily Berkman/Sandbox 22024-04-16T19:28:48Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
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<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:Superimposed_ramps3.jpg|275 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor. RAMP 1 is in pink, RAMP 2 is in tan, RAMP 3 is in blue, calcitonin receptor is in grey, and amylin is in yellow. pdb: 7TYF (RAMP 1), 7TYX (RAMP 2), 7TZF (RAMP 3).]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps3.jpg&diff=4126910File:Superimposed ramps3.jpg2024-04-16T19:22:38Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps3.png&diff=4126904File:Superimposed ramps3.png2024-04-16T19:12:58Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps.png&diff=4126903File:Superimposed ramps.png2024-04-16T19:12:21Z<p>Emily Berkman: uploaded a new version of "Image:Superimposed ramps.png"</p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126902Emily Berkman/Sandbox 22024-04-16T19:11:52Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed_ramps2.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps2.png&diff=4126901File:Superimposed ramps2.png2024-04-16T19:11:10Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126899Emily Berkman/Sandbox 22024-04-16T19:07:39Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/8'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/4'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126672Emily Berkman/Sandbox 22024-04-11T18:55:52Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126671Emily Berkman/Sandbox 22024-04-11T18:55:25Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126670Emily Berkman/Sandbox 22024-04-11T18:55:13Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126669Emily Berkman/Sandbox 22024-04-11T18:54:52Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
<br />
<br />
<br />
<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
<br />
<br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126668Emily Berkman/Sandbox 22024-04-11T18:53:35Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
[[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]]<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
[[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]]<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps.png&diff=4126667File:Superimposed ramps.png2024-04-11T18:49:11Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Conserved_residues.png&diff=4126665File:Conserved residues.png2024-04-11T18:24:57Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126664Emily Berkman/Sandbox 22024-04-11T18:22:29Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126663Emily Berkman/Sandbox 22024-04-11T18:20:12Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for the stabilization of amylin in the receptor. Threonine side chains are polar which allows them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126662Emily Berkman/Sandbox 22024-04-11T18:13:30Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/7'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4126661Emily Berkman/Sandbox 22024-04-11T18:01:08Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/4'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/4'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/4'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4122757Emily Berkman/Sandbox 22024-04-09T19:59:21Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref><br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/1'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/1'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/4'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4122751Emily Berkman/Sandbox 22024-04-09T19:46:43Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/1'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/1'>C2 and C7</scene> that is conserved across almost every species.<ref name="Bower">PMID:27061187</ref><br />
<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/4'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <ref name="Cao">PMID:35324283</ref><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4122739Emily Berkman/Sandbox 22024-04-09T19:36:23Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered, through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy], that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/1'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/1'>C2 and C7</scene> that is conserved across almost every species.<br />
<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/4'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4122731Emily Berkman/Sandbox 22024-04-09T19:32:43Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain/4'>T9 Water Network Main Chain</scene><br />
<br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
<scene name='10/1038871/Rat_pram_19/1'>residue 19 changes</scene><br />
<br />
==Introduction==<br />
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analogue of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered, through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy], that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<br />
==Amylin==<br />
Amylin is extremely conserved among species, in order to maintain proper structure and function. Some of the main <scene name='10/1038871/Conserved_residues/1'>conserved residues</scene> are Lysine 1, Cysteine 2, Alanine 5, Threonine 6, and Cysteine 7. All of the conserved residues exhibit extensive hydrogen bonding networks between either other residues or surrounding water molecules. There is also a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='10/1038871/Disulfide/1'>C2 and C7</scene> that is conserved across almost every species.<br />
==T9==<br />
Threonine 9 is an essential residue for stabilization of amylin in the receptor. Threonine side chains are polar which allow them to hydrogen bond with other nearby polar groups, which can lead to extensive networks of interactions. This is seen in amylin at T9. T9 interacts with the <scene name='10/1038871/T9_main_chain/4'>main chain atoms</scene> of Y191, M230, I380, and H381 of the [https://en.wikipedia.org/wiki/Calcitonin_receptor calcitonin receptor] and many surrounding water molecules, but it also interacts with the <scene name='10/1038871/T9_network/1'>side chain atoms</scene> of S159, N194, S195, H226, N233, and Q383. All of these interactions create a very strong interaction between amylin and the receptor. The water network also helps stabilize the active receptor conformation. <br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4122696Emily Berkman/Sandbox 22024-04-09T18:33:09Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain/4'>T9 Water Network Main Chain</scene><br />
<br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
<scene name='10/1037520/Rat_pram_template/1'>rat pram template</scene><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4115910Emily Berkman/Sandbox 22024-04-02T20:04:31Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain/4'>T9 Water Network Main Chain</scene><br />
<br />
<scene name='10/1038871/Superimposed_ramps/1'>superimposed ramps</scene><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:Superimposed_ramps.pdb&diff=4115890File:Superimposed ramps.pdb2024-04-02T19:33:04Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109461Emily Berkman/Sandbox 22024-03-26T20:10:20Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain/4'>T9 Water Network Main Chain</scene><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109460Emily Berkman/Sandbox 22024-03-26T20:09:17Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain/3'>T9 Water Network Main Chain</scene><br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109459Emily Berkman/Sandbox 22024-03-26T20:05:21Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network Side Chain Interactions</scene><br />
<br />
<scene name='10/1038871/T9_main_chain_almost_done/1'>T9 Main Chain</scene><br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109451Emily Berkman/Sandbox 22024-03-26T19:48:37Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<scene name='10/1038871/T9_network/1'>T9 Water Network</scene><br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109440Emily Berkman/Sandbox 22024-03-26T19:20:17Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved_residues/1'>Conserved Residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109438Emily Berkman/Sandbox 22024-03-26T19:18:20Z<p>Emily Berkman: </p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<scene name='10/1038871/Conserved Residues/1'>Conserved residues</scene><br />
<br />
<scene name='10/1038871/Disulfide/1'>Disulfide</scene><br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_2&diff=4109424Emily Berkman/Sandbox 22024-03-26T18:22:11Z<p>Emily Berkman: New page: ==amylin images== <StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''> </StructureSection> == References == <references/></p>
<hr />
<div>==amylin images==<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=User:Emily_Berkman&diff=4109423User:Emily Berkman2024-03-26T18:21:28Z<p>Emily Berkman: </p>
<hr />
<div>* Full Real Name:Emily Berkman<br />
<br />
* Position:Student<br />
<br />
* Institution (NO ABBREVIATIONS):Butler University<br />
<br />
* City, State/Province, Country:Indianapolis, IN, USA<br />
<br />
* Field of Expertise or Study:Biochemistry<br />
<br />
*[[Emily Berkman/Sandbox 1]]<br />
<br />
*[[Emily Berkman/Sandbox 2]]</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4102036Emily Berkman/Sandbox 12024-03-19T19:56:56Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='350' frame='true' side='right' caption='Amylin, 7TZF' scene=''><br />
==Introduction==<br />
Amylin<ref name="Cao">PMID:35324283</ref> is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
<scene name='10/1037515/Calcitonin_residues_200-210/1'>Calcitonin Section</scene><br />
<br />
===Important Residues===<br />
C2-C7 [https://en.wikipedia.org/wiki/Disulfide disulfide bond]<br />
<br />
==Function==<br />
Amylin helps regulate glucose homeostasis. <ref name="Ransey">PMID:28504306</ref><br />
<br />
[[Image:t9 full 2.png|400 px|left|thumb|Figure 1. Zoomed out look at the amylin water network at the N-Terminal end.]]<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4102025Emily Berkman/Sandbox 12024-03-19T19:46:21Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='350' frame='true' side='right' caption='Amylin, 7TZF' scene=''><br />
==Introduction==<br />
Amylin is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
<scene name='10/1037515/Calcitonin_residues_200-210/1'>Calcitonin Section</scene><br />
<br />
===Important Residues===<br />
C2-C7 [https://en.wikipedia.org/wiki/Disulfide disulfide bond]<br />
<br />
==Function==<br />
Amylin helps regulate glucose homeostasis. <br />
<br />
[[Image:t9 full 2.png|400 px|left|thumb|Figure 1. Zoomed out look at the amylin water network at the N-Terminal end.]]<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4102024Emily Berkman/Sandbox 12024-03-19T19:44:37Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='350' frame='true' side='right' caption='Amylin, 7TZF' scene='Calcitonin Residues 200-210'><br />
==Introduction==<br />
Amylin is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
<scene name='10/1037515/Calcitonin_residues_200-210/1'>Calcitonin Section</scene><br />
<br />
===Important Residues===<br />
C2-C7 [https://en.wikipedia.org/wiki/Disulfide disulfide bond]<br />
<br />
==Function==<br />
Amylin helps regulate glucose homeostasis. <br />
<br />
[[Image:t9 full 2.png|400 px|left|thumb|Figure 1. Zoomed out look at the amylin water network at the N-Terminal end.]]<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101998Emily Berkman/Sandbox 12024-03-19T19:19:52Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='350' frame='true' side='right' caption='Amylin, 7TZF' scene=''><br />
==Introduction==<br />
Amylin is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
===Important Residues===<br />
C2-C7 [https://en.wikipedia.org/wiki/Disulfide disulfide bond]<br />
<br />
==Function==<br />
Amylin helps regulate glucose homeostasis. <br />
<br />
[[Image:t9 full 2.png|400 px|left|thumb|Figure 1. Zoomed out look at the amylin water network at the N-Terminal end.]]<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=File:T9_full_2.png&diff=4101980File:T9 full 2.png2024-03-19T19:07:40Z<p>Emily Berkman: </p>
<hr />
<div></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101969Emily Berkman/Sandbox 12024-03-19T19:03:02Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
==Introduction==<br />
Amylin is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
===Important Residues===<br />
C2-C7 disulfide bond. <br />
<br />
==Function==<br />
Amylin helps regulate glucose homeostasis. <br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101965Emily Berkman/Sandbox 12024-03-19T19:00:44Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
==Introduction==<br />
Amylin is a neuroendocrine hormone found in many species. <br />
<br />
==Main Structure==<br />
Amylin is found embedded in the membrane of organisms. <br />
<br />
===Structural Highlights===<br />
Binds to RAMP.<br />
<br />
===Important Residues===<br />
C2-C7 disulfide bond. <br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101961Emily Berkman/Sandbox 12024-03-19T18:58:20Z<p>Emily Berkman: </p>
<hr />
<div>=Amylin with AMY3-R, 7TZF=<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
==Introduction==<br />
<br />
==Main Structure==<br />
<br />
=== Structural Highlights ===<br />
<br />
=== Important Residues ===<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101955Emily Berkman/Sandbox 12024-03-19T18:53:31Z<p>Emily Berkman: </p>
<hr />
<div>=Rat Amylin, 7TZF=<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
==Introduction==<br />
<br />
==Main Structure==<br />
<br />
=== Structural Highlights ===<br />
<br />
=== Important Residues ===<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
== Student Contributors ==<br />
*Emily Berkman<br />
*Brynn Baker<br />
*Sepp Hall</div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101947Emily Berkman/Sandbox 12024-03-19T18:50:10Z<p>Emily Berkman: </p>
<hr />
<div>=Rat Amylin, 7TZF=<br />
<StructureSection load='7tzf' size='340' side='right' caption='Caption for this structure' scene=''><br />
<br />
==Introduction==<br />
<br />
This is a default text for your page '''Emily Berkman/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
== Function ==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkmanhttps://proteopedia.org/index.php?title=Emily_Berkman/Sandbox_1&diff=4101940Emily Berkman/Sandbox 12024-03-19T18:40:15Z<p>Emily Berkman: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...</p>
<hr />
<div>==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Emily Berkman/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
== Function ==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Emily Berkman