Conformational Control of Integrin‐Subtype Selectivity in isoDGR Peptide Motifs: A Biological Switch

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 α5β1 integrin (see the docking model) with an aff...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2010-11, Vol.49 (48), p.9278-9281
Main Authors: Frank, Andreas O, Otto, Elke, Mas‐Moruno, Carlos, Schiller, Herbert B, Marinelli, Luciana, Cosconati, Sandro, Bochen, Alexander, Vossmeyer, Dörte, Zahn, Grit, Stragies, Roland, Novellino, Ettore, Kessler, Horst
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Binding Sites
cyclic pentapeptides
Enginyeria dels materials
Fibronectins
Humans
Integrin alphaVbeta3 - chemistry
integrin ligands
isoDGR sequence
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides - chemistry
Peptide Fragments - chemistry
Peptides
Protein Structure, Tertiary
Pèptids
Receptors, Vitronectin - chemistry
Àrees temàtiques de la UPC
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Summary: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 α5β1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201004363