Sandbox Reserved 1451: Difference between revisions

Line 30:

[[Image:7tm labeled.png|right|300px]]

Up until 2007, rhodopsin was the only GPCR that had a high-resolution crystal structure and was the basis for other GPCR structures<ref name="Article2">“RHO Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, 11AD, ghr.nlm.nih.gov/gene/RHO#.</ref>. Most G-protein coupled receptors are a target for pharmaceutical companies as the receptors are involved in a variety of physiological and pathophysiological processes<ref name="Article3">PMID:21352497</ref>. Most GPCRs bind ligands with an open domain. Rhodopsin and other vision proteins are unique as the proteins acquire ligands via transient pores in that open between the transmembrane helices of the GPCR. The use of transient pores allows thermal stability of the rhodopsin protein<ref name="Article4">PMID:29042326</ref>.

== Structural highlights ==

<scene name='77/778331/Rhodopsin_no_ligand/1'>Rhodopsin protein</scene> Fully functional rhodopsin has the typical GPCR structure of a seven transmembrane helical bundle with the N-terminus on the interior of the rods and the C-terminus in the cytoplasm. The N-terminus is located near the extracellular loops and ends of the transmembrane protein. There are hydrogen bonding between the transmembrane sections and the extracellular loops that are involved in the activation of rhodopsin when a photon is received. The N-terminus is thought to play a role in orientation of the extracellular loops<ref name="Article4">PMID:29042326</ref>. Transmembrane domain 1 and 2 play a role in stabilizing the protein and giving the protein functionality<ref name="Article3">PMID:21352497</ref>. Rhodopsin has two components: opsin (a membrane-bound polypeptide) and 11-cis-retinal (a chromophore that is bound to opsin via a protonated Schiff-base)<ref name="Article5">PMID:12402507</ref>.

Sandbox Reserved 1451: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 30: / Line 30: @@
 [[Image:7tm labeled.png|right|300px]]
 Up until 2007, rhodopsin was the only GPCR that had a high-resolution crystal structure and was the basis for other GPCR structures<ref name="Article2">“RHO Gene - Genetics Home Reference.” U.S. National Library of Medicine, National Institutes of Health, 11AD, ghr.nlm.nih.gov/gene/RHO#.</ref>. Most G-protein coupled receptors are a target for pharmaceutical companies as the receptors are involved in a variety of physiological and pathophysiological processes<ref name="Article3">PMID:21352497</ref>. Most GPCRs bind ligands with an open domain. Rhodopsin and other vision proteins are unique as the proteins acquire ligands via transient pores in that open between the transmembrane helices of the GPCR. The use of transient pores allows thermal stability of the rhodopsin protein<ref name="Article4">PMID:29042326</ref>.
+== Structural highlights ==
+<scene name='77/778331/Rhodopsin_no_ligand/1'>Rhodopsin protein</scene> Fully functional rhodopsin has the typical GPCR structure of a seven transmembrane helical bundle with the N-terminus on the interior of the rods and the C-terminus in the cytoplasm. The N-terminus is located near the extracellular loops and ends of the transmembrane protein. There are hydrogen bonding between the transmembrane sections and the extracellular loops that are involved in the activation of rhodopsin when a photon is received. The N-terminus is thought to play a role in orientation of the extracellular loops<ref name="Article4">PMID:29042326</ref>. Transmembrane domain 1 and 2 play a role in stabilizing the protein and giving the protein functionality<ref name="Article3">PMID:21352497</ref>. Rhodopsin has two components: opsin (a membrane-bound polypeptide) and 11-cis-retinal (a chromophore that is bound to opsin via a protonated Schiff-base)<ref name="Article5">PMID:12402507</ref>.