Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9- cis retinal.
First-pass extracted concept
jumping spider rhodopsin-1
Candidate: toolkit item1 source documents4 linked claims
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Compared with bovine rhodopsin, jumping spider rhodopsin-1 adopts a more activation-ready transmembrane bundle conformation similar to bistable squid rhodopsin and other nonphotosensitive class A GPCRs.
Quoted textsource-backed
In contrast to bovine rhodopsin (monostable), the transmembrane bundle of jumping spider rhodopsin-1 as well that of the bistable squid rhodopsin adopts a more “activation-ready” conformation often observed in other nonphotosensitive class A GPCRs.
A water-mediated network around the ligand in jumping spider rhodopsin-1 may underlie its bistable nature.
Quoted textsource-backed
We observe a water-mediated network around the ligand hinting toward the basis of their bistable nature.
Jumping spider rhodopsin-1 may serve as a model system for studying structure-function relationships of photosensitive and nonphotosensitive class A GPCRs.
Quoted textsource-backed
These similarities suggest the role of jumping spider rhodopsin-1 as a potential model system in the study of the structure–function relationship of both photosensitive and nonphotosensitive class A GPCRs.
The paper reports a high-resolution crystal structure of recombinant jumping spider rhodopsin-1 bound to 9-cis retinal.
Quoted textsource-backed
Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9- cis retinal.