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Analysis of the MCTP Amino Acid Sequence Reveals the Conservation of Putative Calcium- and Lipid-Binding Pockets Within the C2 Domains In Silico. | LitMetric
Department of Biomedical and Clinical Sciences (BKV), Linköping University, 581 83, Linköping, Sweden.
Published: August 2022
AI Article Synopsis
MCTPs (Multiple C2 Domains and Transmembrane region Proteins) are related to other important proteins involved in processes like exocytosis and membrane trafficking, but their specific functions have not been thoroughly researched.
They are found in endosomes and the endoplasmic reticulum, featuring three conserved C2 domains and two transmembrane regions across different species.
Structural modeling and docking analysis of MCTP's C2 domains in C. elegans suggests they have calcium- and lipid-binding abilities, indicating that MCTPs likely play a crucial, calcium-dependent role in membrane function.
Article Abstract
MCTPs (Multiple C2 Domains and Transmembrane region Proteins) are evolutionarily and structurally related to other C2 proteins, which are central to exocytosis and membrane trafficking; however, their specific function has been little studied. MCTPs are associated with endosomes and the endoplasmic reticulum and possess three C2 domains (C2A-C2C) and two transmembrane regions (TMRs) well conserved in different species. Here, we generated structural models of the MCTP C2 domains of C. elegans and analyzed their putative function by docking, which revealed that these domains possess Ca- and lipid-binding pockets, suggesting that MCTPs play a significant, calcium-dependent role in membrane physiology.
