Effects of D128N Mutation on OsSERK2 in Xa21-Mediated Immune Complex: An In Silico Study

Figure 2

Changes in interactions of prominent residues of the complex. (a) Arg185 and Arg 230 of Xa21 form hydrogen bonds with Leu52 of OsSERK2 and Asp6 of RaxX21-sY in the wild complex. (b) Val2 and Lys15 of RaxX21-sY form hydrogen bonds with Asn331 and Cys382 of Xa21 in the wild complex. (c) Lys164 of OsSERK2 forms an ionic bond with Asp565 of Xa21 in the wild complex. (d) Arg185 of Xa21 discontinues the previous interaction, and Arg230 of Xa21 forms a new hydrogen bond with Asp56 of OsSERK2 D128N in the mutated complex (Table S2). (e) Val2 and Lys15 of RaxX21-sY form a new hydrophobic interaction with Phe354 and hydrogen bond Asn383 of Xa21 in the mutated complex (Tables S2 and S3). (f) Lys164 of OsSERK2 D128N shows no interaction within 4.0 Å in the mutated complex. Cartoon: Xa21-RaxX21-sY-OsSERK2 complex where Xa21 (magenta), RaxX21-sY (blue), and OsSERK2 (green), and Xa21-RaxX21-sY-OsSERK2 D128N complex where Xa21 (light blue), RaxX21-sY (yellow), and OsSERK2 D128N (orange); stick: prominent and interacting residues of both complex; all the complexes were investigated after 100 ns MD simulation.