The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Titolo: | Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch |
Autori: | |
Data di pubblicazione: | 2010 |
Rivista: | |
Abstract: | The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
Handle: | http://hdl.handle.net/11591/188549 |
Appare nelle tipologie: | 1.1 Articolo in rivista |
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