Many cellular proteins are methylated at lysine residues, which have been most intensively studied for histone proteins. Eukaryotic elongation factor 1A (eEF1A) is an essential, highly methylated protein. It is a crucial translational elongation factor that can be found in all living organisms, together with its bacterial homolog EF-Tu. The main function of eEF1A is to facilitate the delivery of aminoacyl-tRNA to the ribosome. In addition, it also plays a role in many other cellular process such as actin bundling, nuclear export and proteasomal degradation. A number of methyltransferases targeting translation elongation factors have been identified in both S. cerevisiae and humans. In yeast, four of these elongation factor methyltransferases (EFMs) act on eEF1A, namely Efm1, Efm4, Efm5 and Efm6, to produce monomethylated Lys. Nowadays, eEF1A plays an important role in viral replication, and scientists have suggested that eEF1A may be a promising target for anti-coronavirus drugs. Considering that, BOC Sciences provides a specialized library for screening compounds that target eEF1A.
Figure 1. A model of the eEF1 complex. (Shuhei, S.; et al. 2018)
eEF1A Targeted Library Design
- Our teams can create a high-quality structural model when there is no available X-ray data for eEF1A
- A docking-based virtual screening is carried out for the design of an eEF1A targeted library
- We mainly apply two different binding sites on the surface eEF1A for docking: GTP-binding site and the eEF1B⍺-binding site, which allow us to select nearly 3,000 promising ligands that have high predicted affinity to eEF1A
- These ligands meet the Ro5 criteria and do not contain PAINS, toxic or reactive moieties
- No docking constraints have been employed
eEF1A Targeted Library Characteristics
- Bioactivity and safety confirmed by preclinical studies and clinical trials
- Structural diversity, medicinal activity, and cellular penetration
- Structural document, IC50, and other chemical and biological data are provided
- All compounds are continually updated
- Compound cherry-picking service is provided
Figure 2. Localization of the residues of motif Post II in the active site of eEF1A-KMT4. (Jakobsson, M. E.; et al. 2017)
What We Deliver
- Delivered within 2 weeks in any customer-preferred format
- Powders, dry films or DMSO solutions formatted in vials, 96 or 384-well plates
- All compounds have a minimum purity of 90% assessed by 1H NMR and HPLC
- Analytical data is provided
BOC Sciences provides professional, rapid and high-quality services of eEF1A Targeted Library design at competitive prices for global customers. Personalized and customized services of eEF1A Targeted Library design can satisfy any innovative scientific study demands. Our clients have direct access to our staff and prompt feedback to their inquiries. If you are interested in our services, please contact us immediately!
References
- Shuhei, S.; et al. Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins. Frontiers in Microbiology. 2018. 9:1446.
- Jakobsson, M. E.; et al. Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation. Nucleic Acids Research. 2017. 45(14): 8239-8254.
