1PWV
Crystal structure of Anthrax Lethal Factor wild-type protein complexed with an optimised peptide substrate.
Summary for 1PWV
| Entry DOI | 10.2210/pdb1pwv/pdb |
| Related | 1PQW 1PWP 1PWU 1PWW |
| Descriptor | Lethal factor, LF20 (2 entities in total) |
| Functional Keywords | anthrax toxin, lethal factor, optimised peptide substrate, hydrolase |
| Biological source | Bacillus anthracis More |
| Cellular location | Secreted: P15917 |
| Total number of polymer chains | 4 |
| Total formula weight | 185423.29 |
| Authors | Wong, T.Y.,Schwarzenbacher, R.,Liddington, R.C. (deposition date: 2003-07-02, release date: 2004-02-03, Last modification date: 2023-08-16) |
| Primary citation | Turk, B.E.,Wong, T.Y.,Schwarzenbacher, R.,Jarrell, E.T.,Leppla, S.H.,Collier, R.J.,Liddington, R.C.,Cantley, L.C. The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Nat.Struct.Mol.Biol., 11:60-66, 2004 Cited by PubMed Abstract: Recent events have created an urgent need for new therapeutic strategies to treat anthrax. We have applied a mixture-based peptide library approach to rapidly determine the optimal peptide substrate for the anthrax lethal factor (LF), a metalloproteinase with an important role in the pathogenesis of the disease. Using this approach we have identified peptide analogs that inhibit the enzyme in vitro and that protect cultured macrophages from LF-mediated cytolysis. The crystal structures of LF bound to an optimized peptide substrate and to peptide-based inhibitors provide a rationale for the observed selectivity and may be exploited in the design of future generations of LF inhibitors. PubMed: 14718924DOI: 10.1038/nsmb708 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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