| pubmed-article:16756510 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16756510 | lifeskim:mentions | umls-concept:C0035499 | lld:lifeskim |
| pubmed-article:16756510 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
| pubmed-article:16756510 | pubmed:dateCreated | 2006-6-7 | lld:pubmed |
| pubmed-article:16756510 | pubmed:abstractText | The rhodopsin crystal structure provides a structural basis for understanding the function of this and other G protein-coupled receptors (GPCRs). The major structural motifs observed for rhodopsin are expected to carry over to other GPCRs, and the mechanism of transformation of the receptor from inactive to active forms is thus likely conserved. Moreover, the high expression level of rhodopsin in the retina, its specific localization in the internal disks of the photoreceptor structures [termed rod outer segments (ROS)], and the lack of other highly abundant membrane proteins allow rhodopsin to be examined in the native disk membranes by a number of methods. The results of these investigations provide evidence of the propensity of rhodopsin and, most likely, other GPCRs to dimerize, a property that may be pertinent to their function. | lld:pubmed |
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