Journalartikel

Jahr der Veröffentlichung: 2001

Seiten: 783-794

Zeitschrift: Journal of Molecular Biology

Bandnummer: 312

Heftnummer: 4

ISSN: 0022-2836

eISSN: 1089-8638

DOI Link: https://doi.org/10.1006/jmbi.2001.4989

Verlag: Elsevier

Abstract: 
Listeria monocytogenes is an opportunistic, food-borne human and animal pathogen. Host cell invasion requires the action of the internalins A (In1A) and B (In1B), which are members of a family of listerial cell-surface proteins. Common to these proteins are three distinctive N-terminal domains that have been shown to direct host cell-specific invasion for In1A and In1B. Here, we present the high-resolution crystal structures of these domains present in In1B and In1H, and show thai they constitute a single "internalin domain". In this internalin domain, a central LRR region is flanked contiguously by a truncated EF-hand-like cap and an immunoglobulin (1g)-like fold. Tl e extended P-sheet, resulting from the distinctive fusion of the LRR and the Ig-like folds, constitutes an adaptable concave interaction surface, which we propose is responsible for the specific recognition of the host cellular binding partners during infection. (C) 2001 Academic Press.

Harvard-Zitierstil: Schubert, W., Göbel, G., Diepholz, M., Darji, A., Kloer, D., Hain, T., et al. (2001) Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain, Journal of Molecular Biology, 312(4), pp. 783-794. https://doi.org/10.1006/jmbi.2001.4989

APA-Zitierstil: Schubert, W., Göbel, G., Diepholz, M., Darji, A., Kloer, D., Hain, T., Chakraborty, T., Wehland, J., Domann, E., & Heinz, D. (2001). Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. Journal of Molecular Biology. 312(4), 783-794. https://doi.org/10.1006/jmbi.2001.4989