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IMAGE: UTSW scientists have characterized three different conformations of alpha 7, a key cell-surface protein. view more
Credit: Leah Baxter
DALLAS - March 17, 2021 - UT Southwestern researchers have identified the structure of a key member of a family of proteins called nicotinic acetylcholine receptors in three different shapes. The work, published online today in
Cell, could eventually lead to new pharmaceutical treatments for a large range of diseases or infections including schizophrenia, lung cancer, and even COVID-19.
Nicotinic acetylcholine receptors are members of a broader super-family of proteins called Cys-loop receptors that function as ion channels on cell surfaces and are found in the membranes of many cell types. When the right molecule settles on these receptors, it opens the gated channels, letting ions flood from the outside to the inside of cells to trigger other cellular processes. Nicotinic acetylcholine receptors respond to acetylchol
Credit: UT Southwestern Medical Center
DALLAS - Feb. 11, 2021 - A study led by UT Southwestern has identified a mechanism that controls the activity of proteins known as chaperones, which guide proteins to fold into the right shapes. The findings, published online today in
Nature Communications, could shed light on hundreds of degenerative and neurodegenerative diseases caused by protein misfolding, such as Alzheimer s, Parkinson s, and Huntington s, potentially leading to new treatments for these devastating conditions.
Every protein in the body is originally produced in a linear chain, with amino acid building blocks strung together one after another. But to fulfill their roles in cells, explains study leader Lukasz Joachimiak, Ph.D., assistant professor in the Center for Alzheimer s and Neurodegenerative Diseases at UT Southwestern, these chains need to fold into precise shapes. Chaperones help proteins accomplish this by protecting their vulnerable portions while they shift i