X-ray crystallographic fragment screening reveals novel and conformationally dynamic ligand-binding sites in Mycobacterium tuberculosis FtsZ
Kaylen R. Meeks, Edwin O. Lazo, Dale F. Kreitler · 2026
Read X-ray crystallographic fragment screening reveals novel and conformationally dynamic ligand-binding sites in Mycobacterium tuberculosis FtsZ by Kaylen R. Meeks, Edwin O. Lazo, Dale F. Kreitler (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13684551.txt.
Description
Kaylen Meeks, Edwin Lazo, and Dale Kreitler screen small molecule fragments against a tuberculosis protein, in a 2026 paper. The protein FtsZ is essential for bacterial cell division, making it an attractive drug target. Fragment screening finds weak binders that can later be grown into real drugs.
The team soaked more than a thousand crystals with fragments and analyzed hundreds of datasets. Many showed clear fragment binding, and they describe fifteen new binding sites. The protein appeared in both its on and off shapes in the same crystal, and fragments bound unevenly to its two copies. The results open routes to build FtsZ blockers and shape-specific probes.
Catalog record
| CREATOR | Kaylen R. Meeks, Edwin O. Lazo, Dale F. Kreitler |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 41 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |