How Does Protonation Change The Structure Of Carbonate
Protonation states at dissimilar pH, conformational changes and bear upon of glycosylation in synapsin Ia†
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Abstract
Synapsin I (SynI) is the most abundant brain phosphoprotein present at presynaptic terminals that regulates neurotransmitter release, clustering of synaptic vesicles (SVs) at active zones, and stimulates synaptogenesis and neurite outgrowth. Before studies have established that SynI displays pH-dependent tethering of SVs to actin filaments and exhibits a maximum binding around neutral pH, nevertheless, the effect of pH shift from acidic to basic on the conformational stability of SynI has not been explored yet. Another of import attribute of SynIa is its O-GlcNAcylation (O-GlcNac) at the Thr87 position, which is responsible for the positive regulation of synaptic plasticity linked to learning and memory in mice. Furthermore, reduced levels of O-GlcNAc have been observed in Alzheimer's disease, suggesting a possible link to deficits in synaptic plasticity. In this written report, the effect of pH and glycosylation on the structure and functional stability of SynIa is determined through molecular dynamics (MD) simulation approach. The 3D structure of SynIa was established via threading-based homology modeling methods. It was observed that the structure of SynIa adopts extended conformational changes as the pH shifts from acidic to bones, resulting in a meaty conformation at pH eight.0. Moreover, the results obtained by comparing the glycosylated and unglycosylated protein indicated that the glycan moiety imparts stability to the protein by forming intramolecular hydrogen bond interactions with the poly peptide residues. The results indicate that although O-GlcNAc moieties practise not induce a significant change in SynIa structure they minimize protein dynamics, probable leading to enhanced poly peptide stability.
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Supplementary files
- Supplementary information PDB (4986K)
- Supplementary data PDB (4984K)
- Supplementary information PDB (844K)
- Supplementary information PDB (4983K)
- Supplementary data PDF (501K)
Article information
- DOI
- https://doi.org/10.1039/D1CP00531F
- Article type
- Paper
- Submitted
- 04 Feb 2021
- Accepted
- 05 Jul 2021
- First published
- 06 Jul 2021
Phys. Chem. Chem. Phys. , 2021, 23, 16718-16729
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Protonation states at different pH, conformational changes and impact of glycosylation in synapsin Ia
S. Mir, Due south. Ashraf, K. Saeed, A. Rahman and Z. Ul-Haq, Phys. Chem. Chem. Phys., 2021,23, 16718 DOI: 10.1039/D1CP00531F
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Source: https://pubs.rsc.org/en/content/articlelanding/2021/cp/d1cp00531f
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