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Mechanisms of Ligand–Protein Interaction in Sec-14-like Transporters Investigated by Computer Simulations

Type of publication Peer-reviewed
Publikationsform Review article (peer-reviewed)
Author Helbling Rachel E., Lamprakis Christos, Aeschimann Walter, Bolze Cristin S., Stocker Achim, Cascella Michele,
Project The role of CRALBP in the chemistry of vision
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Review article (peer-reviewed)

Journal CHIMIA International Journal for Chemistry
Volume (Issue) 68(9)
Page(s) 615 - 619
Title of proceedings CHIMIA International Journal for Chemistry
DOI 10.2533/chimia.2014.615

Open Access

Type of Open Access Website


We review our recent work on protein-ligand interactions in vitamin transporters of the Sec-14-like protein. Our studies focused on the cellular-retinaldehyde binding protein (CRALBP) and the alpha-tocopherol transfer protein (alpha-TTP). CRALBP is responsible for mobilisation and photo-protection of short-chain cis-retinoids in the dim-light visual cycle or rod photoreceptors. alpha-TTP is a key protein responsible for selection and retention of RRR-alpha-tocopherol, the most active isoform of vitamin E in superior animals. Our simulation studies evidence how subtle chemical variations in the substrate can lead to significant distortion in the structure of the complex, and how these changes can either lead to new protein function, or be used to model engineered protein variants with tailored properties. Finally, we show how integration of computational and experimental results can contribute in synergy to the understanding of fundamental processes at the biomolecular scale.