Sandbox Reserved 1852: Difference between revisions
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:Glu 162, a <scene name='10/1075254/Q162/5'>glutamine</scene>, resides near the top of the binding site, and is about than 3Å from the ligand in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, Glu162 was mutated to an <scene name='10/1075254/Q_to_r/2'>arginine</scene>, which decreased the length of the potential hydrogen bond to within 2.5Å in most models, increasing the strength of the interaction.<ref name="Siegel"/> | :Glu 162, a <scene name='10/1075254/Q162/5'>glutamine</scene>, resides near the top of the binding site, and is about than 3Å from the ligand in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, Glu162 was mutated to an <scene name='10/1075254/Q_to_r/2'>arginine</scene>, which decreased the length of the potential hydrogen bond to within 2.5Å in most models, increasing the strength of the interaction.<ref name="Siegel"/> | ||
=====S284A===== | =====S284A===== | ||
:Ser 284 resides deep within the binding pocket of the enzyme. Choosing a <scene name='10/1075254/S284/2'>serine</scene> to <scene name='10/1075254/A285_scence/ | :Ser 284 resides deep within the binding pocket of the enzyme. Choosing a <scene name='10/1075254/S284/2'>serine</scene> to <scene name='10/1075254/A285_scence/3'>alanine</scene> mutation increases the hydrophobicity of the binding pocket and reduce reactivity, without also changing any steric characteristics in the region ''unintentionally'' near the catalytic residues.<ref name="Siegel"/> | ||
=====A285N===== | =====A285N===== | ||
:<scene name='10/1075254/N285/5'>Asp285</scene>, as follows, is also buried within the binding pocket. Introducing this mutation increases steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.<ref name="Siegel"/> | :<scene name='10/1075254/N285/5'>Asp285</scene>, as follows, is also buried within the binding pocket. Introducing this mutation increases steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.<ref name="Siegel"/> | ||
