Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain
| Autor: | Katherine E. Lobel-Rice, Alexander Sorkin, Royston E. Carter, Michael Overduin, Tonny de Beer |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Protein Folding Stereochemistry Protein Conformation Molecular Sequence Data Mineralogy Plasma protein binding Biology Ligands Protein Structure Secondary Protein structure Amino Acid Sequence Binding site Peptide sequence Nuclear Magnetic Resonance Biomolecular Multidisciplinary Binding Sites EF hand Binding protein Calcium-Binding Proteins Helix-Loop-Helix Motifs Phosphoproteins Mutation Protein folding Calcium Oligopeptides Alpha helix Protein Binding Signal Transduction |
| Zdroj: | Science (New York, N.Y.). 281(5381) |
| ISSN: | 0036-8075 |
| Popis: | Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second of which binds tightly to calcium. The NPF peptide is bound in a hydrophobic pocket between two α helices, and binding is mediated by a critical aromatic interaction as revealed by structure-based mutagenesis. The fold is predicted to be highly conserved among 30 identified EH domains and provides a structural basis for defining EH-mediated events in protein trafficking and growth factor signaling. |
| Databáze: | OpenAIRE |
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