1EH2
STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES
Summary for 1EH2
| Entry DOI | 10.2210/pdb1eh2/pdb |
| NMR Information | BMRB: 4184 |
| Descriptor | EPS15, CALCIUM ION (2 entities in total) |
| Functional Keywords | calcium binding, signaling domain, npf binding, ef-hand, eh domain |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm. Isoform 2: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side: P42566 |
| Total number of polymer chains | 1 |
| Total formula weight | 11975.89 |
| Authors | De Beer, T.,Carter, R.E.,Lobel-Rice, K.E.,Sorkin, A.,Overduin, M. (deposition date: 1998-07-10, release date: 1999-07-22, Last modification date: 2024-05-22) |
| Primary citation | de Beer, T.,Carter, R.E.,Lobel-Rice, K.E.,Sorkin, A.,Overduin, M. Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science, 281:1357-1360, 1998 Cited by PubMed Abstract: 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 alpha 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. PubMed: 9721102DOI: 10.1126/science.281.5381.1357 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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