Sandbox Reserved 957: Difference between revisions
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Q site contains:<br \> | Q site contains:<br \> | ||
* In particular the conserved residues Gln817, Phe820, Val782 and Tyr612. [24]<br \> | * In particular the conserved residues <scene name='60/604476/Qsite1/1'>Gln817, Phe820, Val782 and Tyr612. [24]</scene><br \> | ||
* The hydrogen bonds, between Gln817 and 775, Gln775 and Ala767, Gln775 and Trp853, imply an interaction between Gln817 and the cGMP purine. Thus, it improves the specificity for the cGMP, against cAMP. [24]<br \> | * The hydrogen bonds, between <scene name='60/604476/Qsite2/1'>Gln817 and 775, Gln775 and Ala767, Gln775 and Trp853</scene>, imply an interaction between <scene name='60/604476/Gln817/1'>Gln817</scene> and the cGMP purine. Thus, it improves the specificity for the cGMP, against cAMP. [24]<br \> | ||
* And Tyr612, Val782, Leu785 an Phe820 bind the cGMP through this pyrazol ring and π-π interactions between Gln817 and the phenyl ring. [24]<br \> | * And <scene name='60/604476/Qsite3/1'>Tyr612, Val782, Leu785 an Phe820</scene> bind the cGMP through this pyrazol ring and π-π interactions between Gln817 and the phenyl ring. [24]<br \> | ||
** So, the conserved hydrophobic residue Tyr 612 is critical in the maintaining of the affinity. [3]<br \> | ** So, the conserved hydrophobic residue <scene name='60/604476/Tyr612/1'>Tyr 612</scene> is critical in the maintaining of the affinity. [3]<br \> | ||
H site:<br \> | H site:<br \> | ||