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

Helbling, Rachel E.; Lamprakis, Christos; Aeschimann, Walter; Bolze, Cristin S.; Stocker, Achim; Cascella, Michele (2014). Mechanisms of Ligand–Protein Interaction in Sec-14-like Transporters Investigated by Computer Simulations. CHIMIA, 68(9), pp. 615-619. Bern: Schweizerische Chemische Gesellschaft 10.2533/chimia.2014.615

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Lamprakis, Christos; Aeschimann, Walter; Stocker, Achim and Cascella, Michele

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry
000 Computer science, knowledge & systems

ISSN:

0009-4293

Publisher:

Schweizerische Chemische Gesellschaft

Language:

English

Submitter:

Achim Stocker

Date Deposited:

24 Oct 2014 16:34

Last Modified:

31 Aug 2015 08:29

Publisher DOI:

10.2533/chimia.2014.615

URI:

https://boris.unibe.ch/id/eprint/59579

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