5DRN
Context-independent anti-hypusine antibody FabHpu24 in complex with hypusine
Summary for 5DRN
| Entry DOI | 10.2210/pdb5drn/pdb |
| Related | 5DS8 5DSC 5DTF 5DUB |
| Descriptor | Fab Hpu24 Heavy chain, Fab Hpu24 Light chain, Hypusine, ... (5 entities in total) |
| Functional Keywords | hypusine, antibody, fabhpu24, eif5a, immune system |
| Biological source | Oryctolagus cuniculus More |
| Total number of polymer chains | 4 |
| Total formula weight | 91874.32 |
| Authors | Zhai, Q.,Carter, P.J. (deposition date: 2015-09-16, release date: 2016-01-20, Last modification date: 2023-11-15) |
| Primary citation | Zhai, Q.,He, M.,Song, A.,Deshayes, K.,Dixit, V.M.,Carter, P.J. Structural Analysis and Optimization of Context-Independent Anti-Hypusine Antibodies. J.Mol.Biol., 428:603-617, 2016 Cited by PubMed Abstract: Context-independent anti-hypusine antibodies that bind to the post-translational modification (PTM), hypusine, with minimal dependence on flanking amino acid sequences, were identified. The antibodies bind to both hypusine and deoxyhypusine or selectively to hypusine but not to deoxyhypusine. Phage display was used to further enhance the affinity of the antibodies. Affinity maturation of these anti-hypusine antibodies improved their performance in affinity capture of the only currently known hypusinated protein, eukaryotic translation initiation factor 5A. These anti-hypusine antibodies may have utility in the identification of novel hypusinated proteins. Crystal structures of the corresponding Fab fragments were determined in complex with hypusine- or deoxyhypusine-containing peptides. The hypusine or deoxyhypusine moiety was found to reside in a deep pocket formed between VH and VL domains of the Fab fragments. Interaction between the antibodies and hypusine includes an extensive hydrogen bond network. These are, to our knowledge, the first reported structures of context-independent anti-PTM antibodies in complex with the corresponding PTM. PubMed: 26778617DOI: 10.1016/j.jmb.2016.01.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.994 Å) |
Structure validation
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