Analysis of the MCTP Amino Acid Sequence Reveals the Conservation of Putative Calcium- and Lipid-Binding Pockets Within the C2 Domains In Silico
Journal of Molecular Evolution, ISSN: 1432-1432, Vol: 90, Issue: 3-4, Page: 271-282
2022
- 4Citations
- 1Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations4
- Citation Indexes4
- Captures1
- Readers1
Article Description
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.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85130527263&origin=inward; http://dx.doi.org/10.1007/s00239-022-10057-1; http://www.ncbi.nlm.nih.gov/pubmed/35604448; https://link.springer.com/10.1007/s00239-022-10057-1; https://dx.doi.org/10.1007/s00239-022-10057-1; https://link.springer.com/article/10.1007/s00239-022-10057-1
Springer Science and Business Media LLC
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