Sandbox Reserved 1165: Difference between revisions

Line 23:

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 binding pocket 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 disulfide bond between Cys 294 and Cys 224 mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the 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 stalk 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 binding pocket 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 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 stalk is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.

Sandbox Reserved 1165: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 01:57, 25 March 2016 view source Steven Bennett (talk \| contribs) 218 edits No edit summary ← Older edit		Revision as of 23:33, 28 March 2016 view source Sydney Caskey (talk \| contribs) 73 edits No edit summary Newer edit →
Line 23:		Line 23:

	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 binding pocket 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 disulfide bond between Cys 294 and Cys 224 mentioned earlier that serves to hold the ECL1 and ECL2 in the proper orientation. Additionally, the 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 stalk 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 binding pocket 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 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 stalk is imperative to the affinity and binding of the glucagon <ref name="Tips">PMID: 23863937</ref>.