Structural characterization of a URB597–FAAH conjugate
Biochemical assay · Purified humanized rat FAAH (h/rFAAH), transmembrane-deleted construct spanning amino acids 30–579 with six active-site substitutions to human residues. [1]
X-ray crystallography characterized the reported h/rFAAH–URB597 conjugate at 2.30 Å resolution. This is a structural experiment with an engineered enzyme, rather than a cellular potency or native human FAAH experiment.
| Endpoint | Reported result | Reference |
|---|---|---|
| Resolution of the FAAH–URB597 crystal structure | X-ray structure resolution 2.30 Å | [1] |
Literature-Reported Treatment Conditions
- Exposure duration
- Inhibitor was added after the first purification step and incubated at 4°C overnight.
- Method
- In vitro preparation of an enzyme–inhibitor conjugate for crystallography.
- Reported limits
- URB597 concentration and inhibitor stock vehicle are not specified in the acquired shared methods. These conditions do not describe a cellular treatment or animal dose.
Methods and source locations
Compound reported in the paper: URB597
Reported structural result for URB597 with engineered h/rFAAH; no Adooq material, cellular activity, animal efficacy or clinical effect established.
Results, opening paragraph; Table 1, FAAH–URB597 column; Materials and Methods, FAAH Expression and Purification and Crystallization and Crystal Structure Determination
Resolution of the FAAH–URB597 crystal structure: X-ray diffraction from a single crystal; molecular replacement and crystallographic refinement. Table 1 reports a data-collection range of 30.0–2.30 Å and refinement resolution of 2.30 Å. — Table 1, FAAH–URB597 column, Resolution rows; Results, opening paragraph