9CCE
structure of DYNA_1b7
Summary for 9CCE
| Entry DOI | 10.2210/pdb9cce/pdb |
| Descriptor | DYNA_1b7, Dynorphin A(1-17) (2 entities in total) |
| Functional Keywords | de novo design, deep learning, disorder peptide, protein-peptide complex, de novo protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 4 |
| Total formula weight | 54696.10 |
| Authors | |
| Primary citation | Wu, K.,Jiang, H.,Hicks, D.R.,Liu, C.,Muratspahic, E.,Ramelot, T.A.,Liu, Y.,McNally, K.,Kenny, S.,Mihut, A.,Gaur, A.,Coventry, B.,Chen, W.,Bera, A.K.,Kang, A.,Gerben, S.,Lamb, M.Y.,Murray, A.,Li, X.,Kennedy, M.A.,Yang, W.,Song, Z.,Schober, G.,Brierley, S.M.,O'Neill, J.,Gelb, M.H.,Montelione, G.T.,Derivery, E.,Baker, D. Design of intrinsically disordered region binding proteins. Science, 389:eadr8063-eadr8063, 2025 Cited by PubMed Abstract: Intrinsically disordered proteins and peptides play key roles in biology, but a lack of defined structures and high variability in sequence and conformational preferences have made targeting such systems challenging. We describe a general approach for designing proteins that bind intrinsically disordered protein regions in diverse extended conformations with side chains fitting into complementary binding pockets. We used the approach to design binders for 39 highly diverse unstructured targets, including polar targets, and obtained designs with 100-picomolar to 100-nanomolar affinities in 34 cases, testing ~22 designs per target. The designs function in cells and as detection reagents and are specific for their intended targets in all-by-all binding experiments. Our approach is a major step toward a general solution to the intrinsically disordered protein and peptide recognition problem. PubMed: 40674483DOI: 10.1126/science.adr8063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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