2LDA
Solution structure of the estrogen receptor-binding stapled peptide SP2 (Ac-HKXLHQXLQDS-NH2)
Summary for 2LDA
| Entry DOI | 10.2210/pdb2lda/pdb |
| Related | 2LDC 2LDD |
| NMR Information | BMRB: 17657 |
| Descriptor | Estrogen receptor-binding stapled peptide SP2 (1 entity in total) |
| Functional Keywords | de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 1386.64 |
| Authors | Phillips, C.,Bazin, R.,Bent, A.,Davies, N.,Moore, R.,Pannifer, A.,Pickford, A.,Prior, S.,Read, C.,Roberts, L.,Schade, M.,Scott, A.,Brown, D.,Xu, B.,Irving, S. (deposition date: 2011-05-20, release date: 2011-07-06, Last modification date: 2023-11-15) |
| Primary citation | Phillips, C.,Roberts, L.R.,Schade, M.,Bazin, R.,Bent, A.,Davies, N.L.,Moore, R.,Pannifer, A.D.,Pickford, A.R.,Prior, S.H.,Read, C.M.,Scott, A.,Brown, D.G.,Xu, B.,Irving, S.L. Design and structure of stapled peptides binding to estrogen receptors. J.Am.Chem.Soc., 133:9696-9699, 2011 Cited by PubMed Abstract: Synthetic peptides that specifically bind nuclear hormone receptors offer an alternative approach to small molecules for the modulation of receptor signaling and subsequent gene expression. Here we describe the design of a series of novel stapled peptides that bind the coactivator peptide site of estrogen receptors. Using a number of biophysical techniques, including crystal structure analysis of receptor-stapled peptide complexes, we describe in detail the molecular interactions and demonstrate that all-hydrocarbon staples modulate molecular recognition events. The findings have implications for the design of stapled peptides in general. PubMed: 21612236DOI: 10.1021/ja202946k PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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