http://www.cnr.it/ontology/cnr/individuo/prodotto/ID273020
Structural and dynamical properties of KTS-disintegrins: A comparison between Obtustatin and Lebestatin (Articolo in rivista)
- Type
- Label
- Structural and dynamical properties of KTS-disintegrins: A comparison between Obtustatin and Lebestatin (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bip.22138 (literal)
- Alternative label
Daidone, Isabella; Aschi, Massimiliano; Patamia, Maria; Bozzi, Argante; Petruzzelli, Raffaele (2013)
Structural and dynamical properties of KTS-disintegrins: A comparison between Obtustatin and Lebestatin
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Daidone, Isabella; Aschi, Massimiliano; Patamia, Maria; Bozzi, Argante; Petruzzelli, Raffaele (literal)
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- ISI Web of Science (WoS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- University of Aquila; Catholic University of the Sacred Heart; Consiglio Nazionale delle Ricerche (CNR); University of Aquila; G d'Annunzio University of Chieti-Pescara (literal)
- Titolo
- Structural and dynamical properties of KTS-disintegrins: A comparison between Obtustatin and Lebestatin (literal)
- Abstract
- Obtustatin and Lebestatin are lysine-threonine-serine (KTS)-disintegrins, which are a family of low molecular weight polypeptides present in many viperidae venoms and are potent and specific inhibitors of collagen-binding integrins. The integrin binding loop, harboring the 21KTS23 motif, and the C-terminal tail are known to be responsible for the selective binding to the a1 beta 1 integrin. Despite a very high sequence homology (only two mutations are present in Lebestatin relative to Obtustatin, namely R24L and S38L), Lebestatin exhibits a higher inhibitory effect than Obtustatin on cell adhesion and cell migration to collagens I and IV. Here we show, by means of molecular dynamics simulations of the two polypeptides in aqueous solution, that Lebestatin possesses a higher flexibility of the C-terminal tail and a greater solvent accessibility of the integrin binding loop than Obtustatin. It may be hypothesized that these properties may contribute to the higher binding-affinity of Lebestatin to its biological partner. (c) 2012 Wiley Periodicals, Inc. (literal)
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