Structural and Functional Mimicry of the Binding Site of hYAP-WW Domain for Proline-rich Ligands |
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Authors: | Ulf Strijowski Tatjana Hirsch Aina Quintilla Wolfgang Wenzel Jutta Eichler |
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Affiliation: | (1) Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany;(2) Research Centre Karlsruhe, Institute for Nanotechnology, Karlsruhe, Germany |
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Abstract: | Based on the 3D structure of the WW domain of human Yes-associated protein (hYAP-WW) in complex with a proline-rich peptide ligand, we have designed and synthesized a cyclic peptide covering a fragment of hYAP-WW that contains its primary contact residues for the interaction with the ligand. This peptide was found to specifically recognize a proline-rich ligand for hYAP-WW. Its conformation was calculated using molecular dynamics simulation, based on long-range NOEs identified by NMR spectroscopy, and indicates an arrangement of primary contact residues similar to hYAP-WW. |
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Keywords: | WW domain structure-based design proteinmimetics biomimetic synthesis proline-rich ligands |
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