| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_2a819eda0adf22936a52362eeebb9fb4
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d21cbff64022f95c237c0bd3ec8656ca |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12R2001-445
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-50
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12R2001-16
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-21 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K1-13
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y304-22
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P21-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-52
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K19-00 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-52
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-195
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-31
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-34 |
| filingDate |
2019-05-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_26b48ed3686155548c3ac679585b1f41
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5db660dfc8c0fd527f30e4c017005eab
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0afe7e48c0d14266d0cf99443cbc0684
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_019869aa2eb316ca24453a50981f853a
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_021a12ed2b35c0dac5fc29d737ab46e4
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_af3097e0e374c534c25c0b619b98e7d0 |
| publicationDate |
2019-11-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
WO-2019213262-A9 |
| titleOfInvention |
Reagent to label proteins via lysine isopeptide bonds |
| abstract |
Covalently cross-linked pilus polymers displayed on the cell surface of Gram-positive bacteria are assembled by class C sortase enzymes. These pilus-specific transpeptidases located on the bacterial membrane catalyze a two-step protein ligation reaction - first, cleaving the LPXTG motif of one pilin protomer to form an acyl-enzyme intermediate, and second, joining the terminal threonine to the nucleophilic lysine residue residing within the pilin motif of another pilin protomer. Informed by the high-resolution crystal structures of corynebacterial pilus-specific sortase (SrtA) and by developing structural variants of the sortase enzyme whose catalytic pocket has been unmasked by activating mutations, we have developed new reagents capable of forming isopeptide bonds in vitro. The reagents disclosed herein can catalyze ligation of isolated SpaA domains in vitro provide a facile and versatile new platform for protein engineering and bio-conjugation that has major implications for biotechnology. |
| priorityDate |
2018-05-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |