Binding site of AChR: Difference between revisions
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The superposition of the HAP on loop 182–193 of AChBP reveals the α-BTX to fit exquisitely into the interface of two subunits of the pentameric AChBP. | The superposition of the HAP on loop 182–193 of AChBP reveals the α-BTX to fit exquisitely into the interface of two subunits of the pentameric AChBP. | ||
Loop 2 of the toxin is inserted into the interface of two adjacent subunits of AChBP with relatively minor clashes between AChBP and α-BTX. | Loop 2 of the toxin is inserted into the interface of two adjacent subunits of AChBP with relatively minor clashes between AChBP and α-BTX. | ||
The possible formation of an intermolecular salt bridge between AChR and α-BTX at that positionmay provide further explanation to the high affinity of binding of the toxin to the receptor.This notion is supported by recent studies on charge reversal mutations of basic residues on loop 2 of α-neurotoxin | The possible formation of an intermolecular salt bridge between AChR and α-BTX at that positionmay provide further explanation to the high affinity of binding of the toxin to the receptor.This notion is supported by recent studies on charge reversal mutations of basic residues on loop 2 of α-neurotoxin | ||
So the possible formation of an intermolecular salt bridge between AChR and α-BTX at that position may provide further explanation to the high affinity of binding of the toxin to the receptor. | So the possible formation of an intermolecular salt bridge between AChR and α-BTX at that position may provide further explanation to the high affinity of binding of the toxin to the receptor. | ||
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== Structure of Acetylcholine binding site == | == Structure of Acetylcholine binding site == | ||
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