Sandbox Reserved 1451: Difference between revisions
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[[Image:7tm labeled.png|right| | [[Image:7tm labeled.png|right|200px]] | ||
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>. | 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>. | ||
