Sandbox R.Nithin 6XWD: Difference between revisions
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* '''Domain III (201–303)''': helical region required for dimerization' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | * '''Domain III (201–303)''': helical region required for dimerization' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
== Catalytic Site == | == Catalytic Site == | ||
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Together, these interactions illustrate the principles of Mpro inhibitor design: accurate pocket fitting, hydrogen-bond anchoring in S1, hydrophobic complementarity in S2, and covalent engagement of Cys145. | Together, these interactions illustrate the principles of Mpro inhibitor design: accurate pocket fitting, hydrogen-bond anchoring in S1, hydrophobic complementarity in S2, and covalent engagement of Cys145. | ||
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Overall, covalent inhibition represents a promising antiviral design approach because it combines high selectivity, strong binding, and long-lasting catalytic shutdown. | Overall, covalent inhibition represents a promising antiviral design approach because it combines high selectivity, strong binding, and long-lasting catalytic shutdown. | ||
== Biological Significance == | == Biological Significance == | ||
