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| 001 | 601665 | ||
| 005 | 20250724132719.0 | ||
| 024 | 7 | _ | |a 10.1016/j.ijbiomac.2023.126366 |2 doi |
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| 100 | 1 | _ | |a Wiedemann, C. |0 P:(DE-H253)PIP1100673 |b 0 |
| 245 | _ | _ | |a Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2023 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Macrophage infectivity potentiator (MIP) proteins are widespread in human pathogens including Legionella pneumophila, the causative agent of Legionnaires' disease and protozoans such as Trypanosoma cruzi. All MIP proteins contain a FKBP (FK506 binding protein)-like prolyl-cis/trans-isomerase domain that hence presents an attractive drug target. Some MIPs such as the Legionella pneumophila protein (LpMIP) have additional appendage domains of mostly unknown function. In full-length, homodimeric LpMIP, the N-terminal dimerization domain is linked to the FKBP-like domain via a long, free-standing stalk helix. Combining X-ray crystallography, NMR and EPR spectroscopy and SAXS, we elucidated the importance of the stalk helix for protein dynamics and inhibitor binding to the FKBP-like domain and bidirectional crosstalk between the different protein regions. The first comparison of a microbial MIP and a human FKBP in complex with the same synthetic inhibitor was made possible by high-resolution structures of LpMIP with a [4.3.1]-aza-bicyclic sulfonamide and provides a basis for designing pathogen-selective inhibitors. Through stereospecific methylation, the affinity of inhibitors to L. pneumophila and T. cruzi MIP was greatly improved. The resulting X-ray inhibitor-complex structures of LpMIP and TcMIP at 1.49 and 1.34 Å, respectively, provide a starting point for developing potent inhibitors against MIPs from multiple pathogenic microorganisms. |
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| 700 | 1 | _ | |a Whittaker, J. J. |0 P:(DE-H253)PIP1103412 |b 1 |
| 700 | 1 | _ | |a Pérez Carrillo, V. H. |0 0000-0003-3580-4941 |b 2 |
| 700 | 1 | _ | |a Goretzki, B. |0 P:(DE-H253)PIP1090124 |b 3 |
| 700 | 1 | _ | |a Dajka, M. |b 4 |
| 700 | 1 | _ | |a Tebbe, F. |b 5 |
| 700 | 1 | _ | |a Harder, J.-M. |b 6 |
| 700 | 1 | _ | |a Krajczy, P. R. |b 7 |
| 700 | 1 | _ | |a Joseph, B. |0 0000-0003-4968-889X |b 8 |
| 700 | 1 | _ | |a Hausch, F. |0 P:(DE-H253)PIP1091724 |b 9 |
| 700 | 1 | _ | |a Guskov, A. |0 P:(DE-H253)PIP1019309 |b 10 |
| 700 | 1 | _ | |a Hellmich, Ute |0 P:(DE-H253)PIP1100686 |b 11 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.ijbiomac.2023.126366 |g Vol. 252, p. 126366 - |0 PERI:(DE-600)1483284-7 |p 126366 |t International journal of biological macromolecules |v 252 |y 2023 |x 0141-8130 |
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