4ZG1
Crystal structure of a nanobody raised against KDM5B
Summary for 4ZG1
| Entry DOI | 10.2210/pdb4zg1/pdb |
| Descriptor | NB17 (2 entities in total) |
| Functional Keywords | nanobody, single domain antibody, cdr3 loop, beta sandwich, protein binding |
| Biological source | Lama glama |
| Total number of polymer chains | 6 |
| Total formula weight | 74879.71 |
| Authors | Wiuf, A.,Kristensen, O.,Gajhede, M. (deposition date: 2015-04-22, release date: 2015-05-06, Last modification date: 2024-10-23) |
| Primary citation | Wiuf, A.,Kristensen, L.H.,Kristensen, O.,Dorosz, J.,Jensen, J.,Gajhede, M. Structure and binding properties of a cameloid nanobody raised against KDM5B. Acta Crystallogr.,Sect.F, 71:1235-1241, 2015 Cited by PubMed Abstract: The histone demethylase KDM5B is considered to be a promising target for anticancer therapy. Single-chain antibodies from llama (nanobodies) have been raised to aid in crystallization and structure determination of this enzyme. The antigen-binding properties of 15 of these nanobodies have been characterized. The crystal structure of one of these (NB17) has been determined to a resolution of 1.85 Å. NB17 crystallizes in space group P4322 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximate D3 symmetry with interactions mediated by the CDR loops, which could act as a crystallization nucleus. NB17 does not bind to monomeric KDM5B residues 1-820, but is found to bind to aggregates formed after incubation at 310 K. PubMed: 26457512DOI: 10.1107/S2053230X1501537X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
