Association of CD36 expression and polymorphism with serum biochemical indices in Cherry Valley duck

Dd, Wang; Wg, Li; Yy, Zhang

doi:10.4238/gmr.15027994

Cited by 2 publications

(1 citation statement)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recent research has shown that CD36 is involved in the regulation of calcium levels, phospholipase activation, and eicosanoid generation 8 - 11 . CD36 variants had been associated to blood lipid levels alterations as well to susceptibility to the metabolic modi cations 12,13 .…”

Section: Introductionmentioning

confidence: 99%

The Computational Analyses, Molecular Dynamics of Fatty-Acid Transport Mechanism to the CD36 Receptor: The Outcomes of the Mutation K164A on the Binding Domain, Structure and Function

Akachar

Etchebest

Eljaoudi

et al. 2021

Preprint

View full text Add to dashboard Cite

The transmembrane glycoprotein CD36, which is responsible of the metabolic disorders, and the elevated intake of fat induces lipid buildup, is a multifunctional scavenger receptor signaling those functions in high-affinity tissue uptake of long-chain fatty acids. In this study, we used series of molecular dynamics simulations of the wild type and mutants types K164A CD36 protein interacting with one Palmitic acid (PLM) besides simulations of the wild type interacting with the three PLM to find out the mechanism of the functioning of the complex CD36/Fatty acids and the unraveling of the role of the mutation. Additionally we determined whether Lys164, mostly exposed to protein surface, played important roles in fatty acid uptake. These simulations revealed, the conformational changes induced by Lys164 residue and the altered interactions induced by the mutagenesis of surface lysine that was badly influencing the folding, utility, solubility, and stability form of the variant. Furthermore, Lys164 residue provided the structural basis of forming an opening at the region of principal portal for the dissociation of palmitic acid. The results of our simulations revealed hole two fatty acids found in CD36 cavity structure and it was the most preferred to CD36 structure stabilization.

show abstract

Section: Introductionmentioning

confidence: 99%

The Computational Analyses, Molecular Dynamics of Fatty-Acid Transport Mechanism to the CD36 Receptor: The Outcomes of the Mutation K164A on the Binding Domain, Structure and Function

Akachar

Etchebest

Eljaoudi

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor

Akachar

Etchebest

Jaoudi

et al. 2021

Sci Rep

View full text Add to dashboard Cite

The transmembrane glycoprotein CD36, which is responsible of the metabolic disorders, and the elevated intake of fat induces lipid buildup, is a multifunctional scavenger receptor signaling those functions in high-affinity tissue uptake of long-chain fatty acids. In this study, we used series of molecular dynamics simulations of the wild type and mutants types K164A CD36 protein interacting with one palmitic acid (PLM) besides simulations of the wild type interacting with the three PLM to find out the mechanism of the functioning of the complex CD36/Fatty acids and the unraveling of the role of the mutation. Additionally we determined whether Lys164, mostly exposed to protein surface, played important roles in fatty acid uptake. These simulations revealed, the conformational changes induced by Lys164 residue and the altered interactions induced by the mutagenesis of surface lysine that was badly influencing the folding, utility, solubility, and stability form of the variant. Furthermore, Lys164 residue provided the structural basis of forming an opening at the region of principal portal for the dissociation of palmitic acid. The results of our simulations revealed hole two fatty acids found in CD36 cavity structure and it was the most preferred to CD36 structure stabilization.

show abstract

Association of CD36 expression and polymorphism with serum biochemical indices in Cherry Valley duck

Cited by 2 publications

References 30 publications

The Computational Analyses, Molecular Dynamics of Fatty-Acid Transport Mechanism to the CD36 Receptor: The Outcomes of the Mutation K164A on the Binding Domain, Structure and Function

The Computational Analyses, Molecular Dynamics of Fatty-Acid Transport Mechanism to the CD36 Receptor: The Outcomes of the Mutation K164A on the Binding Domain, Structure and Function

The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor

Contact Info

Product

Resources

About