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- W2044682488 abstract "Repeat proteins, such as ankyrin or leucine-rich repeat proteins, are ubiquitous binding molecules, which occur, unlike antibodies, intra- and extracellularly. Their unique modular architecture features repeating structural units (repeats), which stack together to form elongated repeat domains displaying variable and modular target-binding surfaces. Based on this modularity, we developed a novel strategy to generate combinatorial libraries of polypeptides with highly diversified binding specificities. This strategy includes the consensus design of self-compatible repeats displaying variable surface residues and their random assembly into repeat domains. We envision that such repeat protein libraries will be highly valuable sources for novel binding molecules especially suitable for intracellular applications." @default.
- W2044682488 created "2016-06-24" @default.
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- W2044682488 creator A5090422381 @default.
- W2044682488 date "2003-03-06" @default.
- W2044682488 modified "2023-10-15" @default.
- W2044682488 title "A novel strategy to design binding molecules harnessing the modular nature of repeat proteins" @default.
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- W2044682488 doi "https://doi.org/10.1016/s0014-5793(03)00177-7" @default.
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