In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor
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Date
2021-04Publisher
Brac UniversityAuthor
Naurin, Mehnaz NafisaMetadata
Show full item recordAbstract
Plants that are sessile species are constantly associated with exposure to pathogenic organisms
abundant in their biosphere. Comprehending the hypothesis next to it would be a significant
attempt to study the processes to prevent diseases in plants. In the process, a typical function
of plant-innate immune responses is the identification of disease-causing organisms by pattern
recognition receptors (PRRs). In plants defense system kinase complexes facilitate PRR
signaling at the cell surface, leading to the stimulation of immunological processes which just
treat and prevent the pathogenic invasion. Here, in certain steps, the BRI1-BLD-SERk1(PDB
ID: 4lsx) complex crystallographic structure was designed to simulate for 5ns, as five distinct
collaboration of the core crystallographic structure were included. 5ns simulation model
projections were then reviewed for each arrangement in order to acquire a preview of the
connection as well as immune susceptibility of BRI1 against BLD with the significant help of
co-receptor SERk1. In this analysis, BRI1-BLD-SERK1 complex clearly shows how BLD
operates as a "molecular glue" which facilitates the receptor's interaction with its co-receptor,
which may induce their kinase domains to attach and thereby stimulate the signaling pathway.
The crystal configuration of BRI1-BLD-SERK1 complex further shows that the binding region
for BLD is formed by LRRs 21-25 and together with the island domain. In addition, it was
found that hydrogen-bonding interactions with tyrosine residues in the BRI1 island domain are
formed by BLD. So, any transformation to such BLD attached areas can thus be considered to
be significantly catastrophic to the plant, leading to the inability of the PRR to trace the PAMP.
Since BRI1 has been shown to make a significant contribution in Arabidopsis thaliana's plant
defense system, its hypothesized binding procedure with the BLD and co-receptor SERk1 will
help us to construct a better overview of the initiation phase of PTI.