A new study by chemists at the University of Arkansas shows that X-ray crystallography, the standard method for determining the structure of proteins, can provide inaccurate information about a critical set of proteins – those found in cell membranes – which in turn could be leading to poor and inefficient drug design.
A new study by chemists at the University of Arkansas shows that X-ray crystallography, the standard method for determining the structure of proteins, can provide inaccurate information about a critical set of proteins – those found in cell membranes – which in turn could be leading to poor and inefficient drug design.
The researchers’ findings were published today in Scientific Reports, a Nature publication.
“Two-thirds of all drugs, including those used for chemotherapy, target proteins found on cell membranes,” said Mahmoud Moradi, assistant professor of chemistry and biochemstry in the J. William Fulbright College of Arts and Sciences. “Unfortunately, X-ray crystallography, the gold standard for determining the structure of proteins, has many limitations when dealing with those found in the cellular membrane. Our work exposes, and in many ways, explains these limitations.”
Considered the workhorse molecules of cells, proteins are responsible for nearly every task in living systems. Some proteins live inside cells, and some reside on the cell’s membrane, an outer layer of lipids that separates the cell from its external environment. Membrane proteins are critically important because they regulate the exchange of information and materials between the cell and its environment, a vital task for survival and normal function of the cell because any disorder in protein function can result in disease.
Read more at: University of Arkansas
Computational model YidC2 protein embedded cell membrane. The modeled loop (yellow), missing in the x-ray crystal structure, is crucial for the stabilization of protein. (Photo Credit: Image by Sogol Moradi)
