4R30
Structure of human laforin dual specificity phosphatase domain
Summary for 4R30
| Entry DOI | 10.2210/pdb4r30/pdb |
| Descriptor | Laforin, SULFATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
| Functional Keywords | dual specificity phosphatase, glucan phosphatase, malin, glycogen, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm . Isoform 1: Endoplasmic reticulum. Isoform 2: Endoplasmic reticulum . Isoform 4: Cytoplasm. Isoform 5: Cytoplasm. Isoform 7: Cytoplasm: O95278 |
| Total number of polymer chains | 4 |
| Total formula weight | 85311.22 |
| Authors | Sankhala, R.S.,Koksal, A.C.,Cingolani, G. (deposition date: 2014-08-13, release date: 2014-12-31, Last modification date: 2023-09-20) |
| Primary citation | Sankhala, R.S.,Koksal, A.C.,Ho, L.,Nitschke, F.,Minassian, B.A.,Cingolani, G. Dimeric quaternary structure of human laforin. J.Biol.Chem., 290:4552-4559, 2015 Cited by PubMed Abstract: The phosphatase laforin removes phosphate groups from glycogen during biosynthetic activity. Loss-of-function mutations in the gene encoding laforin is the predominant cause of Lafora disease, a fatal form of progressive myoclonic epilepsy. Here, we used hybrid structural methods to determine the molecular architecture of human laforin. We found that laforin adopts a dimeric quaternary structure, topologically similar to the prototypical dual specificity phosphatase VH1. The interface between the laforin carbohydrate-binding module and the dual specificity phosphatase domain generates an intimate substrate-binding crevice that allows for recognition and dephosphorylation of phosphomonoesters of glucose. We identify novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity. PubMed: 25538239DOI: 10.1074/jbc.M114.627406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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