Emily Berkman/Sandbox 2
From Proteopedia
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==Amylin== | ==Amylin== | ||
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> | 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> | ||
| + | [[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]] | ||
==T9== | ==T9== | ||
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> | 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> | ||
| + | [[Image:superimposed ramps.png|400 px|left|thumb|Figure 2. RAMP 1, 2, and 3 superimposed in the calcitonin receptor.]] | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:53, 11 April 2024
amylin images
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References
- ↑ 1.0 1.1 Bower RL, Hay DL. Amylin structure-function relationships and receptor pharmacology: implications for amylin mimetic drug development. Br J Pharmacol. 2016 Jun;173(12):1883-98. PMID:27061187 doi:10.1111/bph.13496
- ↑ Cao J, Belousoff MJ, Liang YL, Johnson RM, Josephs TM, Fletcher MM, Christopoulos A, Hay DL, Danev R, Wootten D, Sexton PM. A structural basis for amylin receptor phenotype. Science. 2022 Mar 25;375(6587):eabm9609. PMID:35324283 doi:10.1126/science.abm9609
