Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study
Receptor-like kinases (RLKs) are plant proteins that form signaling circuits to transduce information through the plant cell membrane to the nucleus and activate processes that direct growth, development, stress response, and disease resistance. Upon sensing various environmental stress stimuli, RLK...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Hindawi Limited
2023-01-01
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| Series: | Advances in Agriculture |
| Online Access: | http://dx.doi.org/10.1155/2023/2749859 |
| _version_ | 1797403713367703552 |
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| author | Raghib Ishraq Alvy M. H. M. Mubassir Mohd Firdaus Abdul-Wahab Salehhuddin Hamdan |
| author_facet | Raghib Ishraq Alvy M. H. M. Mubassir Mohd Firdaus Abdul-Wahab Salehhuddin Hamdan |
| author_sort | Raghib Ishraq Alvy |
| collection | DOAJ |
| description | Receptor-like kinases (RLKs) are plant proteins that form signaling circuits to transduce information through the plant cell membrane to the nucleus and activate processes that direct growth, development, stress response, and disease resistance. Upon sensing various environmental stress stimuli, RLKs interact with specific targets and recruit several other proteins to initiate the defense mechanism. Among many RLK subfamilies, leucine-rich repeat RLKs (LRR-RLKs) are the largest. Xa21, a member of LRR-RLK, is a vital receptor protein in rice plants that binds with bacterial RaxX21-sY, whereas OsSERK2 is a somatic embryogenic receptor kinase (SERK) that acts as a coreceptor in this process. This study focuses on the effect of a substitution mutation of aspartate128 with asparagine128 (D128N) in OsSERK2 on the interdependent binding pattern of the Xa21, RaxX21-sY, and OsSERK2 D128N proteins. The in silico results showed that the D128N mutation in OsSERK2 can significantly change the interaction pattern of the critical residues of the OsSERK2 and affects its receptor-ligand (Xa21-RaxX21-sY) interaction in the complex. These findings are expected to significantly contribute to the study of the structural basis of Xa21-mediated immunity and the first layer of plant defense mechanisms, thereby aiding further research on these structures and their phenotypic implications. |
| first_indexed | 2024-03-09T02:43:23Z |
| format | Article |
| id | doaj.art-81678a28e6a849359a72ede513e06806 |
| institution | Directory Open Access Journal |
| issn | 2314-7539 |
| language | English |
| last_indexed | 2024-03-09T02:43:23Z |
| publishDate | 2023-01-01 |
| publisher | Hindawi Limited |
| record_format | Article |
| series | Advances in Agriculture |
| spelling | doaj.art-81678a28e6a849359a72ede513e068062023-12-06T00:00:05ZengHindawi LimitedAdvances in Agriculture2314-75392023-01-01202310.1155/2023/2749859Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico StudyRaghib Ishraq Alvy0M. H. M. Mubassir1Mohd Firdaus Abdul-Wahab2Salehhuddin Hamdan3Department of Mathematics and Natural SciencesDepartment of Mathematics and Natural SciencesDepartment of BiosciencesDepartment of BiosciencesReceptor-like kinases (RLKs) are plant proteins that form signaling circuits to transduce information through the plant cell membrane to the nucleus and activate processes that direct growth, development, stress response, and disease resistance. Upon sensing various environmental stress stimuli, RLKs interact with specific targets and recruit several other proteins to initiate the defense mechanism. Among many RLK subfamilies, leucine-rich repeat RLKs (LRR-RLKs) are the largest. Xa21, a member of LRR-RLK, is a vital receptor protein in rice plants that binds with bacterial RaxX21-sY, whereas OsSERK2 is a somatic embryogenic receptor kinase (SERK) that acts as a coreceptor in this process. This study focuses on the effect of a substitution mutation of aspartate128 with asparagine128 (D128N) in OsSERK2 on the interdependent binding pattern of the Xa21, RaxX21-sY, and OsSERK2 D128N proteins. The in silico results showed that the D128N mutation in OsSERK2 can significantly change the interaction pattern of the critical residues of the OsSERK2 and affects its receptor-ligand (Xa21-RaxX21-sY) interaction in the complex. These findings are expected to significantly contribute to the study of the structural basis of Xa21-mediated immunity and the first layer of plant defense mechanisms, thereby aiding further research on these structures and their phenotypic implications.http://dx.doi.org/10.1155/2023/2749859 |
| spellingShingle | Raghib Ishraq Alvy M. H. M. Mubassir Mohd Firdaus Abdul-Wahab Salehhuddin Hamdan Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study Advances in Agriculture |
| title | Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study |
| title_full | Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study |
| title_fullStr | Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study |
| title_full_unstemmed | Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study |
| title_short | Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study |
| title_sort | effects of d128n mutation on osserk2 in xa21 mediated immune complex an in silico study |
| url | http://dx.doi.org/10.1155/2023/2749859 |
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