Sandbox Reserved 1165: Difference between revisions

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Many of the [https://en.wikipedia.org/wiki/Residue_(chemistry) residues] that are in direct contact with the glucagon molecule are [https://en.wikipedia.org/wiki/Ion charged] or are [https://en.wikipedia.org/wiki/Chemical_polarity polar].

There are also many smaller residues on glucagon that support the bulky residues on the GCGR. These residues are located within the <scene name='72/721535/~~Binding_pocket_plain~~/1'>binding pocket</scene> of the 7TM <ref name="Ligands">PMID: 21542831</ref>. There are specific amino acid interactions that hold the helices of the 7TM in the closed conformation that maximizes [http://www.chemicool.com/definition/affinity.html affinity]. This includes a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='72/721535/Disulfide_bond_notspin/1'>Cys 294 and Cys 224</scene> mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] between Glu 406, Arg 173, and Arg 346, also mentioned earlier, hold the conformation together for higher affinity. Finally, alpha helical structure of the <scene name='72/721535/Opening_orientation/2'>stalk</scene> is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.

There are also many smaller residues on glucagon that support the bulky residues on the GCGR. These residues are located within the <scene name='72/721535/Binding_pocket_orange/1'>binding pocket</scene> of the 7TM <ref name="Ligands">PMID: 21542831</ref>. There are specific amino acid interactions that hold the helices of the 7TM in the closed conformation that maximizes [http://www.chemicool.com/definition/affinity.html affinity]. This includes a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='72/721535/Disulfide_bond_notspin/1'>Cys 294 and Cys 224</scene> mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] between Glu 406, Arg 173, and Arg 346, also mentioned earlier, hold the conformation together for higher affinity. Finally, alpha helical structure of the <scene name='72/721535/Opening_orientation/2'>stalk</scene> is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.

Sandbox Reserved 1165: Difference between revisions

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Revision as of 18:17, 29 March 2016 view source Steven Bennett (talk \| contribs) 218 edits No edit summary ← Older edit		Revision as of 19:22, 29 March 2016 view source Sydney Caskey (talk \| contribs) 73 edits No edit summary Newer edit →
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	Many of the [https://en.wikipedia.org/wiki/Residue_(chemistry) residues] that are in direct contact with the glucagon molecule are [https://en.wikipedia.org/wiki/Ion charged] or are [https://en.wikipedia.org/wiki/Chemical_polarity polar].		Many of the [https://en.wikipedia.org/wiki/Residue_(chemistry) residues] that are in direct contact with the glucagon molecule are [https://en.wikipedia.org/wiki/Ion charged] or are [https://en.wikipedia.org/wiki/Chemical_polarity polar].
	There are also many smaller residues on glucagon that support the bulky residues on the GCGR. These residues are located within the <scene name='72/721535/~~Binding_pocket_plain~~/1'>binding pocket</scene> of the 7TM <ref name="Ligands">PMID: 21542831</ref>. There are specific amino acid interactions that hold the helices of the 7TM in the closed conformation that maximizes [http://www.chemicool.com/definition/affinity.html affinity]. This includes a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='72/721535/Disulfide_bond_notspin/1'>Cys 294 and Cys 224</scene> mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] between Glu 406, Arg 173, and Arg 346, also mentioned earlier, hold the conformation together for higher affinity. Finally, alpha helical structure of the <scene name='72/721535/Opening_orientation/2'>stalk</scene> is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.		There are also many smaller residues on glucagon that support the bulky residues on the GCGR. These residues are located within the <scene name='72/721535/Binding_pocket_orange/1'>binding pocket</scene> of the 7TM <ref name="Ligands">PMID: 21542831</ref>. There are specific amino acid interactions that hold the helices of the 7TM in the closed conformation that maximizes [http://www.chemicool.com/definition/affinity.html affinity]. This includes a [https://en.wikipedia.org/wiki/Disulfide disulfide bond] between <scene name='72/721535/Disulfide_bond_notspin/1'>Cys 294 and Cys 224</scene> mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] between Glu 406, Arg 173, and Arg 346, also mentioned earlier, hold the conformation together for higher affinity. Finally, alpha helical structure of the <scene name='72/721535/Opening_orientation/2'>stalk</scene> is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.