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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

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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 Ca2+- and lipid-binding pockets, suggesting that MCTPs play a significant, calcium-dependent role in membrane physiology.

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Acknowledgements

This work was supported by CONACYT A1-S-7659 and PAPIIT-UNAM IN204520 to AMT. José Luis Téllez Arreola is a doctoral student from Programa de Doctorado en Ciencias Biomédicas, Universidad Nacional Autónoma de México (UNAM) and received fellowship 395834 from CONACYT and Fulbright-Garcia Robles (COMEXUS). We thank Meghana Venkatesan for the English edition to the manuscript.

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Correspondence to José Luis Téllez-Arreola or Argel Estrada-Mondragón.

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Téllez-Arreola, J.L., Martínez-Torres, A., Flores-Moran, A.E. et al. Analysis of the MCTP Amino Acid Sequence Reveals the Conservation of Putative Calcium- and Lipid-Binding Pockets Within the C2 Domains In Silico. J Mol Evol 90, 271–282 (2022). https://doi.org/10.1007/s00239-022-10057-1

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