Sandbox Reserved 1451: Difference between revisions

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''Retinitis Pigmentosa''

Retinitis pigmentosa is also an autosomal dominant disorder, but can also be recessive in rare circumstances. There are two main classes of mutations that cause retinitis pigmentosa, class I and class II<ref name="Article4">PMID:29042326</ref>. A mutation that affect rhodopsin that cause retinitis pigmentosa result in a misfolding or transportation of the protein. Class I mutations are commonly associated with a defect in the C-terminus of the protein which results in defective trafficking of the protein<ref name="Article4">PMID:29042326</ref>. Class II mutations are commonly associated with the N-terminus of the protein and results in misfolding in the endoplasmic reticulum<ref name="Article4">PMID:29042326</ref>. Another mutation to rhodopsin can affect the activation of the protein in response to light. These mutations can lead to apoptosis of rods in the retina. Without rods to perceive dim light, night blindness results<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>.

== Relevance ==

[[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>.

Sandbox Reserved 1451: Difference between revisions

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@@ Line 27: / Line 27: @@
 ''Retinitis Pigmentosa''
 Retinitis pigmentosa is also an autosomal dominant disorder, but can also be recessive in rare circumstances. There are two main classes of mutations that cause retinitis pigmentosa, class I and class II<ref name="Article4">PMID:29042326</ref>. A mutation that affect rhodopsin that cause retinitis pigmentosa result in a misfolding or transportation of the protein. Class I mutations are commonly associated with a defect in the C-terminus of the protein which results in defective trafficking of the protein<ref name="Article4">PMID:29042326</ref>. Class II mutations are commonly associated with the N-terminus of the protein and results in misfolding in the endoplasmic reticulum<ref name="Article4">PMID:29042326</ref>. Another mutation to rhodopsin can affect the activation of the protein in response to light. These mutations can lead to apoptosis of rods in the retina. Without rods to perceive dim light, night blindness results<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>.
+== Relevance ==
+[[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>.