7RG8
Crystal Structure of a Stable Heparanase Mutant
Summary for 7RG8
| Entry DOI | 10.2210/pdb7rg8/pdb |
| Descriptor | Heparanase 50 kDa subunit, Heparanase 8 kDa subunit, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | heparanase, heparan sulfate, hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 53794.41 |
| Authors | Whitefield, C.,Hong, N.S.,Jackson, C.J. (deposition date: 2021-07-14, release date: 2022-03-02, Last modification date: 2024-10-30) |
| Primary citation | Whitefield, C.,Hong, N.,Mitchell, J.A.,Jackson, C.J. Computational design and experimental characterisation of a stable human heparanase variant. Rsc Chem Biol, 3:341-349, 2022 Cited by PubMed Abstract: Heparanase is the only human enzyme known to hydrolyse heparin sulfate and is involved in many important physiological processes. However, it is also unregulated in many disease states, such as cancer, diabetes and Covid-19. It is thus an important drug target, yet the heterologous production of heparanase is challenging and only possible in mammalian or insect expression systems, which limits the ability of many laboratories to study it. Here we describe the computational redesign of heparanase to allow high yield expression in . This mutated form of heparanase exhibits essentially identical kinetics, inhibition, structure and protein dynamics to the wild type protein, despite the presence of 26 mutations. This variant will facilitate wider study of this important enzyme and contributes to a growing body of literature that shows evolutionarily conserved and functionally neutral mutations can have significant effects on protein folding and expression. PubMed: 35382258DOI: 10.1039/d1cb00239b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
Download full validation report
