In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor
This thesis is submitted in partial fulfillment of the requirements for the degree of Bachelor of Science in Biotechnology 2021.
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Brac University
2021
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| Առցանց հասանելիություն: | http://hdl.handle.net/10361/14996 |
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10361-149962021-09-13T21:01:20Z In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor Naurin, Mehnaz Nafisa Mubassir, M H M Department of Mathematics and Natural Sciences, Brac University Silico structural analysis The complex BRI1 Receptor BRI1-BLD-SERK1 Pattern Recognition Receptors (PRRs) This thesis is submitted in partial fulfillment of the requirements for the degree of Bachelor of Science in Biotechnology 2021. Catalogued from PDF version of thesis. Includes bibliographical references (pages 27-30). 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. Mehnaz Nafisa Naurin B. Biotechnology 2021-09-13T06:04:05Z 2021-09-13T06:04:05Z 2021 2021-04 Thesis ID: 16136020 http://hdl.handle.net/10361/14996 en_US Brac 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. 30 Pages application/pdf Brac University |
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Brac University |
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Institutional Repository |
| language |
en_US |
| topic |
Silico structural analysis The complex BRI1 Receptor BRI1-BLD-SERK1 Pattern Recognition Receptors (PRRs) |
| spellingShingle |
Silico structural analysis The complex BRI1 Receptor BRI1-BLD-SERK1 Pattern Recognition Receptors (PRRs) Naurin, Mehnaz Nafisa In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| description |
This thesis is submitted in partial fulfillment of the requirements for the degree of Bachelor of Science in Biotechnology 2021. |
| author2 |
Mubassir, M H M |
| author_facet |
Mubassir, M H M Naurin, Mehnaz Nafisa |
| format |
Thesis |
| author |
Naurin, Mehnaz Nafisa |
| author_sort |
Naurin, Mehnaz Nafisa |
| title |
In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| title_short |
In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| title_full |
In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| title_fullStr |
In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| title_full_unstemmed |
In silico structural analysis of the complex BRI1 Receptor like Kinase, Pamp Brassinolide and Serk1 Co-Receptor |
| title_sort |
in silico structural analysis of the complex bri1 receptor like kinase, pamp brassinolide and serk1 co-receptor |
| publisher |
Brac University |
| publishDate |
2021 |
| url |
http://hdl.handle.net/10361/14996 |
| work_keys_str_mv |
AT naurinmehnaznafisa insilicostructuralanalysisofthecomplexbri1receptorlikekinasepampbrassinolideandserk1coreceptor |
| _version_ |
1814307642530594816 |