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In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor

bracu.degree.levelUndergraduate
bracu.type.groupStudent Works
datacite.rightsOpen Access
dc.contributor.advisorMubassir, M H M
dc.contributor.authorNaurin, Mehnaz Nafisa
dc.contributor.departmentDepartment of Mathematics and Natural Sciences
dc.date.accessioned2021-09-13T06:04:05Z
dc.date.available2021-09-13T06:04:05Z
dc.date.copyright2021
dc.date.issued2021-04
dc.descriptionThis thesis is submitted in partial fulfillment of the requirements for the degree of Bachelor of Science in Biotechnology 2021.en_US
dc.descriptionCatalogued from PDF version of thesis.
dc.descriptionIncludes bibliographical references (pages 27-30).
dc.description.abstractPlants 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.en_US
dc.description.degreeBachelor of Science in Biotechnology
dc.description.statementofresponsibilityMehnaz Nafisa Naurin
dc.format.extent30 Pages
dc.identifier.otherID: 16136020
dc.identifier.urihttp://hdl.handle.net/10361/14996
dc.language.isoen_USen_US
dc.publisherBRAC Universityen_US
dc.rightsBrac University theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission.
dc.subjectSilico structural analysisen_US
dc.subjectThe complex BRI1 Receptoren_US
dc.subjectBRI1-BLD-SERK1en_US
dc.subjectPattern Recognition Receptors (PRRs)en_US
dc.titleIn silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptoren_US
dc.typeThesisen_US

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