6n80

S. aureus ClpP bound to anti-4a

spinqualitylabelsall models 6n80, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6n80 is a 14 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.96Å Ligands: JT7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CLPP_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 PubMed Boronic 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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