Comparing transmembrane protein structures with ATOLL

Célien Jacquemard; Guillaume Bret; Thomas Grutter; Esther Kellenberger

doi:10.1093/bioinformatics/btab860

Comparing transmembrane protein structures with ATOLL

Bioinformatics. 2022 Mar 4;38(6):1743-1744. doi: 10.1093/bioinformatics/btab860.

Authors

Célien Jacquemard¹, Guillaume Bret¹, Thomas Grutter², Esther Kellenberger¹

Affiliations

¹ UMR7200 CNRS-Université de Strasbourg, Institut du Médicament de Strasbourg, Faculté de Pharmacie, 67400 Illkirch-Graffenstaden, France.
² UMR7199 CNRS-Université de Strasbourg, Faculté de Pharmacie, 67400 Illkirch-Graffenstaden, France.

PMID: 34954796
DOI: 10.1093/bioinformatics/btab860

Abstract

Summary: The 3D structure of transmembrane helices plays a key role in the function of membrane proteins. While visual inspection can usually discern the distinctive features of a helix bundle, simply translating them into a 2D diagram can be difficult. ATOLL (Aligned Transmembrane dOmains Layout fLattening) projects the helix bundle onto the lipid bilayer plane, thereby facilitating the comparison of different structures of the same membrane protein or structures of different membrane proteins.

Availability and implementation: ATOLL is a program written in Python3. The source code is freely available on the web at https://github.com/LIT-CCM-lab/ATOLL. ATOLL is implemented into a web server (https://atoll.drugdesign.unistra.fr/).

Supplementary information: Supplementary data are available at Bioinformatics online.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Computers*
Membrane Proteins
Software*

Substances

Membrane Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding