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- W2017751246 abstract "Angiogenin and ribonuclease A share 33% sequence identity but have distinct functions. Angiogenin is a potent inducer of angiogenesis that is only weakly ribonucleolytic, whereas ribonuclease A is a robust ribonuclease that is not angiogenic. A chimera (ARH-I), in which angiogenin residues 58-70 are replaced with residues 59-73 of ribonuclease A, has intermediate ribonucleolytic potency and no angiogenic activity. Here we report a crystal structure of ARH-I that reveals the molecular basis for these characteristics. The ribonuclease A-derived (guest) segment adopts a structure largely similar to that in ribonuclease A, and successfully converts this region from a cell-binding site to a purine-binding site. At the same time, its presence causes complex changes in the angiogenin-derived (host) portion that account for much of the increased ribonuclease activity of ARH-I. Guest-host interactions of this type probably occur more generally in protein chimeras, emphasizing the importance of direct structural information for understanding the functional behavior of such molecules." @default.
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- W2017751246 date "2002-07-24" @default.
- W2017751246 modified "2023-09-28" @default.
- W2017751246 title "Guest−Host Crosstalk in an Angiogenin−RNase A Chimeric Protein<sup>,</sup>" @default.
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- W2017751246 doi "https://doi.org/10.1021/bi026151r" @default.
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