Back

Structural basis for the HMGCR interaction with UBIAD1 mutants causing Schnyder corneal dystrophy

Zhou, F.; Weiss, J. S.; Li, W.

2020-06-29 biochemistry
10.1101/2020.06.29.177683 bioRxiv
Show abstract

Schnyder corneal dystrophy (SCD) is an autosomal dominant disease characterized by abnormal deposition of cholesterol and lipid in the cornea. The molecular mechanism underlying this process, which involves the interaction between UBAID1 and HMGCR, remains unclear. Here we investigate these events with in silico approaches. We built the homology models of UBIAD1 and HMGCR based on the existing crystal and cryo-EM structures. The UBIAD1 and HMGCR models are docked and their binding interactions are interrogated by MD simulation. We find that the transmembrane helices of UBIAD1 bind to sterol sensing domain of HMGCR. Upon binding of the GGPP substrate, UBIAD1 shows lower structural flexibility in the TM regions binding to HMGCR. The N102S and G177R mutations disrupts GGPP binding, thereby lowering the binding affinity of HMGCR. Overall, our modeling suggests that SCD mutations in UBIAD1 or lower GGPP concentration increase the structural flexibility of UBIAD1, thereby facilitating its association with HMGCR.Competing Interest StatementThe authors have declared no competing interest.View Full Text

Matching journals

The top 13 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.