6K65
Application of anti-helix antibodies in protein structure determination (9014-1P4B)
Summary for 6K65
| Entry DOI | 10.2210/pdb6k65/pdb |
| Descriptor | Immunoglobulin G-binding protein A, 1P4B variable light chain, 1P4B variable heavy chain, ... (4 entities in total) |
| Functional Keywords | antibody, protein design, structural protein |
| Biological source | Staphylococcus aureus (strain NCTC 8325) More |
| Total number of polymer chains | 3 |
| Total formula weight | 32936.47 |
| Authors | |
| Primary citation | Kim, J.W.,Kim, S.,Lee, H.,Cho, G.,Kim, S.C.,Lee, H.,Jin, M.S.,Lee, J.O. Application of antihelix antibodies in protein structure determination. Proc.Natl.Acad.Sci.USA, 116:17786-17791, 2019 Cited by PubMed Abstract: Antibodies are indispensable tools in protein engineering and structural biology. Antibodies suitable for structural studies should recognize the 3-dimensional (3D) conformations of target proteins. Generating such antibodies and characterizing their complexes with antigens take a significant amount of time and effort. Here, we show that we can expand the application of well-characterized antibodies by "transplanting" the epitopes that they recognize to proteins with completely different structures and sequences. Previously, several antibodies have been shown to recognize the alpha-helical conformation of antigenic peptides. We demonstrate that these antibodies can be made to bind to a variety of unrelated "off-target" proteins by modifying amino acids in the preexisting alpha helices of such proteins. Using X-ray crystallography, we determined the structures of the engineered protein-antibody complexes. All of the antibodies bound to the epitope-transplanted proteins, forming accurately predictable structures. Furthermore, we showed that binding of these antihelix antibodies to the engineered target proteins can modulate their catalytic activities by trapping them in selected functional states. Our method is simple and efficient, and it will have applications in protein X-ray crystallography, electron microscopy, and nanotechnology. PubMed: 31371498DOI: 10.1073/pnas.1910080116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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