ArticleInternational journal of molecular sciences2022
Evolution of the Membrane Transport Protein Domain.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- G-protein-coupled receptor diversity and evolution in the closest living relatives of metazoa.eLife · 2025Article
- Exploring Hormonal Pathways and Gene Networks in Crown Root Formation Under Stress Conditions: An Update.Plants (Basel, Switzerland) · 2025Review
- Biomimetic Diatom Biosilica and Its Potential for Biomedical Applications and Prospects: A Review.International journal of molecular sciences · 2024Review
- Overcoming Biological Barriers: Importance of Membrane Transporters in Homeostasis, Disease and Disease Treatment.International journal of molecular sciences · 2023Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane transport proteins are widely present in all living organisms, however, their function, transported substrate, and mechanism of action are unknown. Here we use diverse bioinformatics tools to investigate the evolution of MTPs, analyse domain organisation and loop topology, and study the comparative alignment of modelled 3D structures. Our results suggest a high level of conservancy between MTPs from different taxa on both amino acids and structural levels, which imply some degree of functional similarities. The presence of loop/s of different lengths in various positions suggests tax-on-specific adaptation to transported substrates, intracellular localisation, accessibility for post-translation modifications, and interaction with other proteins. The comparison of modelled structures proposes close relations and a common origin for MTP and Na/H exchanger. Further, a high level of amino acid similarity and identity between archaeal and bacterial MTPs and Na/H exchangers imply conservancy of ion transporting function at least for archaeal and bacterial MTPs.
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