AlphaFold2 predicts the inward-facing conformation of the multidrug transporter LmrP

By Diego del Alamo, C. Govaerts, Hassane S. Mchaourab. 2021

31 citations recorded by the source corpus.

As part of the CASP competition, the protein structure prediction algorithm AlphaFold2 generated multiple models of the proton/drug antiporter LmrP. Previous distance restraints from double electron‐electron resonance spectroscopy, a technique which reports distance distributions between spin labels attached to proteins, suggest that one of the lower‐ranked models may have captured a conformation that has so far eluded experimental structure determination.

Subfields: Biophysics, Spectroscopy

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In Biophysics

1. Diego del Alamo
2. Jens Meiler
3. Davide Sala
4. Hassane S. Mchaourab

In Spectroscopy

1. Jens Meiler
2. Davide Sala
3. Diego del Alamo
4. Hassane S. Mchaourab

Citations in the corpus

• Sampling alternative conformational states of transporters and receptors with AlphaFold2 (2022, positive): “…we found that AF2 modeled the multidrug transporter LmrP (target T1024) in multiple conformations, two of which were individually consistent with published experimental data ( Jumper et al., 2021b ; Del Alamo et al., 2021a ; Debruycker et al., 2020 ; Martens et al., 2016 ; Masureel et al., 2014 ).”