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dc.contributor.authorHunke, Cornelia
dc.contributor.authorHirsch, Tatjana
dc.contributor.authorEichler, Jutta
dc.date.accessioned2007-06-25T14:52:40Z
dc.date.available2007-06-25T14:52:40Z
dc.date.issued2006-08-01
dc.identifier.citationChembiochem 2006, 7(8):1258-64en
dc.identifier.issn1439-4227
dc.identifier.pmid16810654
dc.identifier.doi10.1002/cbic.200500465
dc.identifier.urihttp://hdl.handle.net/10033/12430
dc.description.abstractThe Mena EVH1 domain, a protein-interaction module involved in actin-based cell motility, recognizes proline-rich ligand motifs, which are also present in the sequence of the surface protein ActA of Listeria monocytogenes. The interaction of ActA with host Mena EVH1 enables the bacterium to actively recruit host actin in order to spread into neighboring cells. Based on the crystal structure of Mena EVH1 in complex with a polyproline peptide ligand, we have generated a range of assembled peptides presenting the Mena EVH1 fragments that make up its discontinuous binding site for proline-rich ligands. Some of these peptides were found to inhibit the interaction of Mena EVH1 with the ligand pGolemi. One of them was further characterized at the level of individual amino acid residues; this yielded information on the contribution of individual positions of the peptides to the interaction with the ligand and identified sites for future structure optimization.
dc.format.extent445080 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.titleStructure-based synthetic mimicry of discontinuous protein binding sites: inhibitors of the interaction of Mena EVH1 domain with proline-rich ligands.en
dc.typeArticleen
dc.format.digYES
refterms.dateFOA2018-06-12T17:43:14Z
html.description.abstractThe Mena EVH1 domain, a protein-interaction module involved in actin-based cell motility, recognizes proline-rich ligand motifs, which are also present in the sequence of the surface protein ActA of Listeria monocytogenes. The interaction of ActA with host Mena EVH1 enables the bacterium to actively recruit host actin in order to spread into neighboring cells. Based on the crystal structure of Mena EVH1 in complex with a polyproline peptide ligand, we have generated a range of assembled peptides presenting the Mena EVH1 fragments that make up its discontinuous binding site for proline-rich ligands. Some of these peptides were found to inhibit the interaction of Mena EVH1 with the ligand pGolemi. One of them was further characterized at the level of individual amino acid residues; this yielded information on the contribution of individual positions of the peptides to the interaction with the ligand and identified sites for future structure optimization.


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