Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch
Journal article published in 2010 by
Andreas O. Frank,
Elke Otto,
Carlos Mas Moruno 
,
Herbert B. Schiller,
Luciana Marinelli,
Sandro Cosconati ,
Alexander Bochen,
Dörte Vossmeyer,
Grit Zahn,
Roland Stragies,
Ettore Novellino,
Horst Kessler
,
Herbert B. Schiller,
Luciana Marinelli,
Sandro Cosconati ,
Alexander Bochen,
Dörte Vossmeyer,
Grit Zahn,
Roland Stragies,
Ettore Novellino,
Horst Kessler
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Abstract
Thumbnail image of graphical 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 a5ß1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide ; Peer Reviewed ; Postprint (published version)