Title : 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.

Pub. Date : 2002 Mar 5

PMID : 11863435






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Steady-state inhibition data show that huprine X binds to human AChE and Torpedo AChE 28- and 54-fold, respectively, more tightly than tacrine. huprine acetylcholinesterase (Cartwright blood group) Homo sapiens
2 Steady-state inhibition data show that huprine X binds to human AChE and Torpedo AChE 28- and 54-fold, respectively, more tightly than tacrine. huprine acetylcholinesterase (Cartwright blood group) Homo sapiens
3 Furthermore, both tacrine and huprine X bind more tightly to Torpedo than to human AChE, suggesting that their quinoline substructures interact better with Phe330 than with Tyr337, the corresponding residue in the human AChE structure. huprine acetylcholinesterase (Cartwright blood group) Homo sapiens
4 Furthermore, both tacrine and huprine X bind more tightly to Torpedo than to human AChE, suggesting that their quinoline substructures interact better with Phe330 than with Tyr337, the corresponding residue in the human AChE structure. huprine acetylcholinesterase (Cartwright blood group) Homo sapiens