The α1-acid glycoprotein (AGP) is an abundant blood plasma protein with important immunomodulatory functions coupled to endogenous and exogenous ligand binding properties. Its affinity for many drug-like structures, however, means AGP can have a significant effect on the pharmokinetics and pharmacodynamics of numerous small molecule therapeutics. Staurosporine, and its hydroxylated forms UCN-01 and UCN-02, are kinase inhibitors that have been investigated at length as anti-tumour compounds. Despite their potency, these compounds display poor pharmokinetics due to binding to both AGP variants, AGP1 and AGP2. Recent renewed interest in UCN-01 as a cytostatic protective agent prompted many structural biologists to solve the structure of the AGP2/UCN-01 complex by X-ray crystallography. Here you can see my personal interpretation of this structure, showing the tight binding to the inhibitor to the catalytic center of the enzyme (PDB code: 7OUB)
#molecularart ... #immolecular ... #tumor .... #antitumoral ... #drug ... #alphaacid ... #glycoprotein ... #xray
Protein-drug complex rendered with @proteinimaging and represented with @corelphotopaint
#molecularart ... #immolecular ... #tumor .... #antitumoral ... #drug ... #alphaacid ... #glycoprotein ... #xray
Protein-drug complex rendered with @proteinimaging and represented with @corelphotopaint
