6VUN
Reverse Transcriptase Diabody with R83C Mutation
Summary for 6VUN
| Entry DOI | 10.2210/pdb6vun/pdb |
| Descriptor | Single-chain Fv, 1,2-ETHANEDIOL, CITRATE ANION, ... (4 entities in total) |
| Functional Keywords | antibody fragment, protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 51608.08 |
| Authors | Chesterman, C.,Arnold, E. (deposition date: 2020-02-16, release date: 2021-02-17, Last modification date: 2024-11-20) |
| Primary citation | Chesterman, C.,Arnold, E. Co-crystallization with diabodies: A case study for the introduction of synthetic symmetry. Structure, 29:598-605.e3, 2021 Cited by PubMed Abstract: This work presents a method for introducing synthetic symmetry into protein crystallization samples using an antibody fragment termed a diabody (Dab). These Dabs contain two target binding sites, and engineered disulfide bonds have been included to modulate Dab flexibility. The impacts of Dab engineering have been observed through assessment of thermal stability, small-angle X-ray scattering, and high-resolution crystal structures. Complexes between the engineered Dabs and HIV-1 reverse transcriptase (RT) bound to a high-affinity DNA aptamer were also generated to explore the capacity of engineered Dabs to enable the crystallization of bound target proteins. This strategy increased the crystallization hit frequency obtained for RT-aptamer, and the structure of a Dab-RT-aptamer complex was determined to 3.0-Å resolution. Introduction of synthetic symmetry using a Dab could be a broadly applicable strategy, especially when monoclonal antibodies for a target have previously been identified. PubMed: 33636101DOI: 10.1016/j.str.2021.02.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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