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
Full text not available from this repository.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 > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) |
UniBE Contributor: |
Lamprakis, Christos, Aeschimann, Walter, Stocker, Achim, 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: |
05 Dec 2022 14:37 |
Publisher DOI: |
10.2533/chimia.2014.615 |
URI: |
https://boris.unibe.ch/id/eprint/59579 |
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