http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-100678425-B1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2299-00 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-16 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-63 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-16 |
| filingDate | 2004-04-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2007-02-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2007-02-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-100678425-B1 |
| titleOfInvention | Crystal Structure of PRL-1 Protein and Method of Crystallization thereof |
| abstract | The present invention relates to the determination of a liver regeneration phosphatase (abbreviated as "PRL") protein and a method for crystallization of the protein, specifically the determination of the PRL-1 protein and i) human-derived Expressing and purifying the PRL-1 protein; ii) crystallizing the protein; And iii) optimizing the protein crystals. The PRL-1 protein crystals of the present invention consist of five strands of beta-sheets surrounded by six alpha-helices, with a well-aligned active site with a closed P-loop, one side As a result, it was confirmed that trimers formed by clustering the C-terminal panicenylation site of each PRL-1 protein molecule were found to be capable of intracellular migration and localization to membrane. The crystal structure of the PRL-1 protein of the present invention can be usefully used for the development of inhibitors that prevent carcinogenesis and cancer metastasis. |
| priorityDate | 2004-04-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 389.