Simulations reveal flexible protein gate controls mitochondrial fold access
Researchers at the Max Delbrück Center and Freie Universität Berlin used computer models to study a human protein complex that regulates entry into mitochondrial folds.
New model explains molecular filter function
A team led by Evangelia Nathanail and Edoardo Rolando created digital simulations of the Mic60-Mic19 subcomplex. These models demonstrate how the structure spans the entrance to cristae deep pockets inside mitochondria. The flexible architecture allows smaller molecules to pass while blocking larger proteins from entering.
Protein complex maintains inner membrane shape
The protein complex called MICOS helps stabilize these internal pockets and acts as a filter for cellular traffic. Disruption of this specific architecture can lead to serious health issues including neurodegenerative diseases and cancer. Scientists published their findings in the journal Nature Communications after running extensive computational experiments.
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