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• W2947997916 abstract "Abstract Lipocalins are potential targets for drug development, and therefore it is important to understand the common and distinct features of their ligand-binding sites. Here, the sequence and structural features of ligand-binding sites in kernel and outlier lipocalins were analyzed and compared. Ligand-binding sites of kernel lipocalins were sequentially more diverse than outlier lipocalins. The ligand-binding sites of the two subgroup lipocalins were relatively hydrophobic and exhibited positive or neutral net-charges, well-correlated with the hydrophobic ligands with neutral or acidic functional groups. There was a propensity of three hydrophobic residues, Phe, Leu and Tyr in the ligand-interacting residues of kernel lipocalins, whereas outlier lipocalins showed relatively lower propensity. Finally, six and ten crucial ligand-interacting positions were identified in the kernel and outlier lipocalins, respectively. These identified features are expected to be a theoretical reference for the engineering and exploration of kernel and outlier lipocalins." @default.
• W2947997916 created "2019-06-07" @default.
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• W2947997916 date "2019-10-01" @default.
• W2947997916 modified "2023-09-24" @default.
• W2947997916 title "Identification of common and distinct features of ligand-binding sites in kernel and outlier lipocalins" @default.
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• W2947997916 doi "https://doi.org/10.1016/j.jiec.2019.05.035" @default.
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