Journal:FEBS Open Bio:2: Difference between revisions
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Ligand binding at each site appeared to be largely determined through hydrophobic interactions. The crystallographic studies support previous conclusions made on ligand binding in noncatalytic sites by ''At''GSTF2 based on isothermal calorimetry experiments (Dixon ''et al''. (2011)<ref>pmid 21631432 </ref>) and suggest a mode of ligand binding in GSTs commensurate with a possible role in ligand transport. | Ligand binding at each site appeared to be largely determined through hydrophobic interactions. The crystallographic studies support previous conclusions made on ligand binding in noncatalytic sites by ''At''GSTF2 based on isothermal calorimetry experiments (Dixon ''et al''. (2011)<ref>pmid 21631432 </ref>) and suggest a mode of ligand binding in GSTs commensurate with a possible role in ligand transport. | ||
Electrostatic surface views of AtGSTF2: | |||
<scene name='76/763766/Cv/23'>Same view as in previous scene, in complex with 2 molecules of S-hexyl glutathione</scene> ([[1gnw]]). | |||
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
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