Weill Cornell Medicine researchers have determined the full-length structure of a blood pressure-regulating hormone receptor for the first time, uncovering how it functions, which may enable better drug targeting of the receptor for diseases such as hypertension and heart failure. For the study, published Nov. 14 in Nature Structural & Molecular Biology, the researchers used cryo-electron microscopy (cryo-EM), computer modeling and other advanced techniques to determine the high-resolution structure of atrial natriuretic peptide receptor 1, also known as transmembrane receptor guanylyl cyclase A (GC-A).
GC-A is a type of single-pass transmembrane receptor protein that spans the cell membrane, connecting a binding region on the cell surface to an interior signaling domain, allowing it to transmit signals from outside the cell to the inside. Basically, the receptor acts as a communication channel between the cell and its environment. “These new structural details will be of interest to drug developers who want to target GC-A and related receptors to treat heart disease and other conditions,” said study senior author Xin-Yun Huang , professor of physiology and biophysics at Weill Cornell Medicine.
The study’s first author, Shian Liu , is a research associate in the department of physiology and biophysics at Weill Cornell Medicine. GC-A is expressed in various tissues – including the kidneys, blood vessels, adrenal glands, lungs, intestines and brain. Its partner hormones.
