Analysis of the MCTP Amino Acid Sequence Reveals the Conservation of Putative Calcium- and Lipid-Binding Pockets Within the C2 Domains In Silico

被引：0
作者：
José Luis Téllez-Arreola
Ataúlfo Martínez-Torres
Adriana E. Flores-Moran
José M. Lazaro-Guevara
Argel Estrada-Mondragón
机构：
[1] Universidad Nacional Autónoma de México,Departamento de Neurobiología Celular Y Molecular, Instituto de Neurobiología
[2] Autonomous University of Queretaro,Unit for Basic and Applied Microbiology, School of Natural Sciences
[3] University of Utah,Department of Human Genetics
[4] University of British Columbia,Department of Botany
[5] University of British Columbia,Biodiversity Research Centre
[6] Linköping University,Department of Biomedical and Clinical Sciences (BKV)
来源：
Journal of Molecular Evolution | 2022年 / 90卷
关键词：
C2 domain; Calcium signaling; Docking; Membrane traffic;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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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页码：271 / 282
页数：11
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