Molecular Models of Peptides

Structural Features in Rhodopsin

Two structures of bovine rhodopsin are shown below. Each consists of the same 308 residue globular protein (an opsin), from which the first 39 residues are removed. The primary structure is listed below, with the missing residues colored red.

MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVF GGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGW SRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWL PYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCM VTTLCCGKNPLGDDEASTTVSKTETSQVAPA
This protein incorporates a retinal chromophore in a binding pocket. The dark adapted case on the left has 11-cis-retinal bound as a Schiff base to Lys 296. In the structure on the right, all-trans-retinal is shown in the same location, partially released from the lysine.
The secondary structure of the protein is significantly different in these examples. Displays of the coiled backbone and/or alpha helices may be turned on and off by the appropriate buttons, as may the locations of the terminal lysine and alanine residues. In many of these displays the retinal chromophore is shown slightly emphasized. The last two buttons bring the retinal moiety into prominence.

Bovine Rhodopsin (dark adapted)
Show Spacefill Model
Show Stick Model
Show Terminal LEU & ALA
Hide Terminal LEU & ALA
Show Backbone Trace
Hide Backbone Trace
Show Helices
Hide Helices
Show 11-cis-Retinal
Back to Protein Complex
Emphasize Retinal and Lysine
Highlight Lysine (protein off)
Bovine Rhodopsin (metarhodopsin II)
 
Show Spacefill Model
Show Stick Model
Show Terminal LEU & ALA
Hide Terminal LEU & ALA
Show Backbone Trace
Hide Backbone Trace
Show Helices
Hide Helices
Show trans-Retinal
Hide trans-Retinal
Emphasize trans-Retinal and Lysine
Show Lysine 296

End of this supplementary topic