Sandbox Reserved 1849: Difference between revisions
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Another important binding site on the RBD includes the Lysine-417 (K417) and Arginine-403 (R403) residues. While <scene name='10/1075250/417_403-ace2-needmeasure/1'>ACE2 does form a hydrogen bond interaction with the K417 residue</scene> using its own D30 residue, LCB1 forms <scene name='10/1075251/D30_lcb1/1'>H bond interactions with both of them</scene>, using its own D30 residue, forming a very strong interaction that is hard to break. | Another important binding site on the RBD includes the Lysine-417 (K417) and Arginine-403 (R403) residues. While <scene name='10/1075250/417_403-ace2-needmeasure/1'>ACE2 does form a hydrogen bond interaction with the K417 residue</scene> using its own D30 residue, LCB1 forms <scene name='10/1075251/D30_lcb1/1'>H bond interactions with both of them</scene>, using its own D30 residue, forming a very strong interaction that is hard to break. | ||
It is important to note that these highlighted residues aren’t the only residues that differ between the minibinders, and it is a compilation of all the residue interactions that give each minibinder different affinities. For example, LCB1 forms no interactions with the Q493 residue of the RDB previously mentioned, yet it still has a higher affinity to the RBD than AHB2 which forms a hydrogen bond with the Q493 residue <ref name="Longxing">PMID:32907861</ref>. | It is important to note that these highlighted residues aren’t the only residues that differ between the minibinders, and it is a compilation of all the residue interactions that give each minibinder different affinities. For example, <scene name='10/1075250/Q493-lcb3/3'>LCB1 forms no interactions with the Q493 residue</scene> of the RDB previously mentioned, yet it still has a higher affinity to the RBD than AHB2 which forms a hydrogen bond with the Q493 residue <ref name="Longxing">PMID:32907861</ref>. | ||
===Function=== | ===Function=== | ||
