PPIST09050
Protein Information
| Protein_Chain | A;B |
|---|---|
| Protein_Sequence | VDLGTENLYFQSNAMKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYGLLLEMLDAHRLHAPTS |
Peptide Information
| Peptide_Chain | C;D |
|---|---|
| Peptide_Sequence | KHKILHRLLQDSS |
| Peptide_Length | 13 |
| Non-standard residues | No |
Interaction Information
| PDB_ID | 4PXM |
|---|---|
| Method | X-RAY DIFFRACTION |
| Resolution | 1.90 angstrom |
| Structure | |
| Protein-peptide residue interaction | |
| Interaction_xlsx | Download interaction table (.xlsx) |
Reference Information
| Title | Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation. |
|---|---|
| Release_Year | 2016 |
| PMID | 26836308 |
| DOI | 10.7554/eLife.12792 |