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• W1562287692 abstract "ABSTRACT Disintegrins, small molecular weight proteins contained in the venom of vipers and rattlesnakes, are high‐affinity and selectivity integrin antagonists. Disintegrins inhibitory epitope mainly consists in a tripeptide sequence localized in a mobile loop protruding from the protein core. RTS and/or KTS tripeptide characterizes the most recently discovered group of disintegrins that selectively block α 1 β 1 integrin receptor. A NMR study dedicated to structure and dynamics properties of jerdostatin, an RTS disintegrin, demonstrated that the substitution of the native RTS with KTS motif impaired flexibility and inhibitory activity of the molecule. Here we add atomic details to the experimental profiles of jerdostatin and its R24K mutant by analyzing the dynamics behavior of the molecules through computational methods. For jerdostatin wild type, molecular dynamics simulations and essential dynamics analyses showed that Y31 residue acts as hinge element in the concerted motions involving the active loop and the C‐terminal tail. R24 side chain ability to engage both cation–π and H‐bond interactions with Y31 residue was found crucial for that breathing mechanism. Less significant loop‐tail concerted motions were observed for the R24K mutant. The description at atomic resolution of jerdostatin dynamics is useful for decoding the influence of specific residues on disintegrin functional properties. © 2014 Wiley Periodicals, Inc. Biopolymers 103: 158–166, 2015." @default.
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• W1562287692 date "2014-12-23" @default.
• W1562287692 modified "2023-10-17" @default.
• W1562287692 title "Essential dynamics analysis captures the concerted motion of the integrin-binding site in jerdostatin, an RTS disintegrin" @default.
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• W1562287692 doi "https://doi.org/10.1002/bip.22578" @default.
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