The human body has about 1,000 kinds
of such receptors, structures on the surface of cells, which let the body respond to a wide variety of chemical signals, like adrenaline.
In cell cultures, the presence of nicotine seemed to increase the number of
such receptors present, but also numbed some of them.
That made researchers worry that small chemicals — which might be just 2 % of a protein's size — would be too puny to turn
on such receptors.
The p75 protein binds to one
such receptor called Ret, which is associated with some neurological conditions as well as certain types of cancer.
Neurogeneticist Ivan Rodriguez of the University of Geneva in Switzerland and colleagues wondered whether there might be
additional such receptors that respond to a disease «scent,» perhaps by detecting chemicals associated with bacteria and inflammation.
A better understanding
of such receptors, he says, may help researchers more efficiently target nicotinelike drugs in patients with diseases that may involve nicotinic receptors, including Parkinson's disease, Tourette's syndrome, and schizophrenia.
«We knew that nicotinic acetylcholine receptors, which bind to the virus in muscles, are also found in the brain, and we presumed that virus could also bind to
such receptors.
Such receptors are natural targets for drug development.
Their experiments with lab - grown mouse and human T - cells suggest that people with cancer who have a greater variety of
such receptors may respond better to immunotherapy drugs and vaccines.
Hu et al. and Zhang et al. use cryo — electron microscopy to uncover the structural and biochemical basis of two
such receptors: NAIP2, which directly binds microbial ligands, and NLRC4, a protein functioning directly downstream.