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- W4250158908 abstract "Membrane proteins are encoded by around one third of a given genome and play key roles in transmission of information and chemicals such as neurotransmitters into the cell. Available membrane protein structures have revealed an abundance of symmetry and pseudo-symmetry, which arose not only by the formation of multi-subunit assemblies, but also by repetition of internal structural elements. In many cases, these symmetry relationships play a crucial role in defining the functional properties of the proteins. In this context, a systematic study of symmetry should provide a framework for a broader understanding of the mechanistic principles and evolutionary development of membrane proteins. However, existing analyses lack the detail and breadth required for such a systematic study. To meet this challenge, we have built a robust symmetry detection methodology that takes into consideration the restrictions that the lipid bilayer places on protein structures. We present the resultant symmetries in an online database called EncoMPASS (encompass.ninds.nih.gov). Using EncoMPASS, we then proceed to quantify both the extent and diversity of symmetry relationships in known structures of membrane proteins. We find that membrane proteins are significantly more enriched in internal symmetry compared to water-soluble proteins. Moreover, when comparing internal symmetries with those between subunits in a complex, we find a striking difference in the preferred orientations of their symmetry axes, indicating an evolutionary bias against dual topology complexes. Our analysis provides a valuable foundation for further investigations into questions relating to the function and evolution of membrane proteins." @default.
- W4250158908 created "2022-05-12" @default.
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- W4250158908 date "2021-02-01" @default.
- W4250158908 modified "2023-09-30" @default.
- W4250158908 title "Systematic Analysis of Symmetry in Membrane Proteins" @default.
- W4250158908 doi "https://doi.org/10.1016/j.bpj.2020.11.1425" @default.
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