Sandbox Reserved 1364

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== References ==
== References ==
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Behnke, Fox, Hori, Kumasaka, Miyano, Motoshima, . . . Palczewski. (1970, January 01). Crystal
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Structure of Bovine Rhodopsin. Retrieved February 21, 2018, from https://www.ebi.ac.uk/pdbe/entry/pdb/1f88
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European Bioinformatics Institute, Protein Information Resource, SIB Swiss Institute of
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Bioinformatics. (2018, January 31). Rhodopsin bos taurus. Retrieved February 21, 2018, from https://www.uniprot.org/uniprot/P02699
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Seeing Zinc. (2004, August 20). Retrieved February 21, 2018, from
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http://www.jbc.org/content/279/34/e99904.full
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Zhou, E. X., Melcher, K., & Xu, E. H. (2012, March). Structure and Activation of Rhodopsin.
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Retrieved February 21, 2018, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677203/

Revision as of 22:16, 21 February 2018

This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430.
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Contents

Bovine Rhodopsin

Bovine Rhodopsin

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PDB: 1f88

Function

Bovine rhodopsin is a G-protein coupled receptor (GCPR) that is responsible for converting light signals into chemical signals that are interpreted by the brain. These visual pigments allow the organism to sense light and is a necessary component of image forming vision at low intensity light. When the protein is exposed to light, it undergoes a conformational change that allows for signal transduction along the molecule. This transduction is facilitated by the binding and unbinding of different molecules, like Zinc, from the numerous binding sites located along the helices. Mutations in the structure are the major cause of vision disorders.

Structural highlights

Rhodopsin is activated when the 11-cis retinal state undergoes isomerization into the all-trans retinal state by photoactivation at the . After a series of related conformational changes, the alpha helices assist the activation of G-protein signaling. The bundle of are an important component of all G-protein coupled receptors, which rhodopsin is. To stabilize the 11-cis retinal ground state, zinc binds to . During photoactivation, the zinc binding is disrupted, and allows easier conformational changes in the retinal site. A decrease in zinc concentration can lead to visual degenerative conditions.


References

Behnke, Fox, Hori, Kumasaka, Miyano, Motoshima, . . . Palczewski. (1970, January 01). Crystal Structure of Bovine Rhodopsin. Retrieved February 21, 2018, from https://www.ebi.ac.uk/pdbe/entry/pdb/1f88

European Bioinformatics Institute, Protein Information Resource, SIB Swiss Institute of Bioinformatics. (2018, January 31). Rhodopsin bos taurus. Retrieved February 21, 2018, from https://www.uniprot.org/uniprot/P02699

Seeing Zinc. (2004, August 20). Retrieved February 21, 2018, from http://www.jbc.org/content/279/34/e99904.full

Zhou, E. X., Melcher, K., & Xu, E. H. (2012, March). Structure and Activation of Rhodopsin. Retrieved February 21, 2018, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677203/

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