3-D atomic structure of TRPML1 ion channel published
Ut Southwestern Medical Center
The illustration shows the studied protein embedded in a nanodisc structure (top left) and three views of the TRPML1 ion channel from different angles. Credit: UT Southwestern UT Southwestern Medical Center researchers today published a 3-D atomic structure of the ion channel found in mammals that is implicated in a rare, inherited neurodegenerative disease in humans. Due to its link to that class of lysosomal storage diseases, TRPML1 has been a potential target for small-molecule therapeutics and several potential agonists (channel openers) have been developed, said Dr. Jiang, a W.W. Caruth, Jr. Scholar in Biomedical Research. Determination of TRPML1’s structure could aid in the search for treatments for mucolipidosis type IV, he said. Working on a team developing what has become one of the top software programs for processing the image data generated by the electron microscopy, Dr. Bai had many conversations with Dr. Richard Henderson, one of three scientists awarded the Nobel Prize in Chemistry last week.