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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 a5ß1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide
Frank, A.O. [et al.]. Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch. "Angewandte chemie. International edition", 2010, vol. 49, núm. 48, p. 9278-9281.