Structural highlights
4hv3 is a 1 chain structure with sequence from Ricinus communis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 1rtc, 1ift, 1br6, 1px8, 1px9, 4esi, 4huo, 4hup, 4hv7 |
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Publication Abstract from PubMed
Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as through X-ray crystallography. Despite the relatively polar, solvent exposed active site, several hydrophobic interactions, most commonly pi-interactions not predicted by modeling programs, were identified in all of the best-performing inhibitors. Nearly all of these compounds provide IC(50) values in the low micromolar range.
Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A.,Saito R, Pruet JM, Manzano LA, Jasheway K, Monzingo AF, Wiget PA, Kamat I, Anslyn EV, Robertus JD J Med Chem. 2012 Dec 19. PMID:23214944[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saito R, Pruet JM, Manzano LA, Jasheway K, Monzingo AF, Wiget PA, Kamat I, Anslyn EV, Robertus JD. Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A. J Med Chem. 2012 Dec 19. PMID:23214944 doi:http://dx.doi.org/10.1021/jm3016393
