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Abb23.7

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Abb23.7

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  1. Abb. 23.7 Vergleich des Bindungsmodus des irreversibel an Thrombin bindenden Inhibitors D-Phe-Pro-Arg-CH2Cl (dunkelrote Kohlenstoffatome) mit dem des Fibrinopeptid-Derivats (graue Kohlenstoffatome). Beide Inhibitoren binden in die S1-Tasche mit einer Argininseitenkette. Die S2-Tasche wird vom Fibrinopeptid durch eine Valinseitenkette besetzt. Seine weitere Peptidkette ist so gefaltet, dass die Seitenketten der an den Positionen P8 und P9 befindlichen Aminosäuren Leu und Phe in die lipophile S3-Bindetasche gerichtet sind. Im Falle des D-Phe-Pro-Arg-CH2Cl bindet der Phenylring des D-Phe in diese Tasche.

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