6n80
From Proteopedia
S. aureus ClpP bound to anti-4a
Structural highlights
FunctionCLPP_STAA8 Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Publication Abstract from PubMedBoronic acids have attracted the attention of synthetic and medicinal chemists due to boron's ability to modulate enzyme function. Recently, we demonstrated that boron-containing amphoteric building blocks facilitate the discovery of bioactive aminoboronic acids. Herein, we have augmented this capability with a de novo library design and virtural screening platform modified for covalent ligands. This technique has allowed us to rapidly design and identify a series of alpha-aminoboronic acids as the first inhibitors of human ClpXP, which is responsible for the degradation of misfolded proteins. De novo design of boron-based peptidomimetics as potent inhibitors of human ClpP in the presence of human ClpX.,Tan J, Grouleff JG, Jitkova Y, Diaz DB, Griffith E, Shao W, Bogdanchikova AF, Poda G, Schimmer AD, Lee RE, Yudin AK J Med Chem. 2019 Jun 12. doi: 10.1021/acs.jmedchem.9b00878. PMID:31187989[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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