English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Objective: To assess protein-protein interactions between fragments of fibrillin-1 protein, whose mutations cause Marfan syndrome (MS). Materials and Methods: We performed a series of protein-protein docking calculations between the macromolecules of interest for this purpose was used Molsoft ICM program. We used the crystal structures of αVβ3 Integrin protein and fragments of fibrillin-1 protein also were generated mutations in the fibrillin-1, which are characteristic in patients with Marfan syndrome and subsequently to the molecular docking. We determined the amino acids most often present at the site of interaction and its hydrophobicity. Results: The amount of hydrophobic amino acids present in the areas of interaction given by the couplings was quantified. Given the energy of the system, was between 40 and 50% of the amino acids of the interaction zone, with a higher proportion relative to charged or neutral amino acids. In the results obtained using the mutations performed on fragments cbEGF23 cbEGF22-TB4-and-cbEGF10 cbEGF9-HYB2 of fibrillin-1, was found they were not placed in areas near the site of interaction in most cases. Conclusion: The interaction between fragments of fibrillin-1, and those with respect to their integrin showed the presence interaction zones mostly hydrophobic amino acids, which are normally expected.

salud/salud uninorte

Study and comparative analysis of interactions protein between the integrina with fragments fibrillin-1 and mutated fragments of this by using molecular docking