5MFC
Designed armadillo repeat protein YIIIM5AII in complex with (KR)4-GFP
Summary for 5MFC
| Entry DOI | 10.2210/pdb5mfc/pdb |
| Descriptor | YIIIM5AII, (KR)4-Green fluorescent protein,Green fluorescent protein, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | designed armadillo repeat protein, peptide binding, de novo protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 4 |
| Total formula weight | 117939.40 |
| Authors | Hansen, S.,Kiefer, J.,Madhurantakam, C.,Mittl, P.,Plueckthun, A. (deposition date: 2016-11-18, release date: 2017-07-19, Last modification date: 2024-11-06) |
| Primary citation | Hansen, S.,Kiefer, J.D.,Madhurantakam, C.,Mittl, P.R.E.,Pluckthun, A. Structures of designed armadillo repeat proteins binding to peptides fused to globular domains. Protein Sci., 26:1942-1952, 2017 Cited by PubMed Abstract: Designed armadillo repeat proteins (dArmRP) are α-helical solenoid repeat proteins with an extended peptide binding groove that were engineered to develop a generic modular technology for peptide recognition. In this context, the term "peptide" not only denotes a short unstructured chain of amino acids, but also an unstructured region of a protein, as they occur in termini, loops, or linkers between folded domains. Here we report two crystal structures of dArmRPs, in complex with peptides fused either to the N-terminus of Green Fluorescent Protein or to the C-terminus of a phage lambda protein D. These structures demonstrate that dArmRPs bind unfolded peptides in the intended conformation also when they constitute unstructured parts of folded proteins, which greatly expands possible applications of the dArmRP technology. Nonetheless, the structures do not fully reflect the binding behavior in solution, that is, some binding sites remain unoccupied in the crystal and even unexpected peptide residues appear to be bound. We show how these differences can be explained by restrictions of the crystal lattice or the composition of the crystallization solution. This illustrates that crystal structures have to be interpreted with caution when protein-peptide interactions are characterized, and should always be correlated with measurements in solution. PubMed: 28691351DOI: 10.1002/pro.3229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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