1o6s
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian | + | Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system. |
==Disease== | ==Disease== | ||
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[[Category: Chakraborty, T.]] | [[Category: Chakraborty, T.]] | ||
[[Category: Domann, E.]] | [[Category: Domann, E.]] | ||
| - | [[Category: Heinz, D | + | [[Category: Heinz, D W.]] |
[[Category: Machner, M.]] | [[Category: Machner, M.]] | ||
| - | [[Category: Schubert, W | + | [[Category: Schubert, W D.]] |
[[Category: Urbanke, C.]] | [[Category: Urbanke, C.]] | ||
[[Category: Wehland, J.]] | [[Category: Wehland, J.]] | ||
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[[Category: leucine rich repeat]] | [[Category: leucine rich repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:08 2008'' |
Revision as of 12:14, 21 February 2008
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INTERNALIN (LISTERIA MONOCYTOGENES) / E-CADHERIN (HUMAN) RECOGNITION COMPLEX
Contents |
Overview
Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.
Disease
Known diseases associated with this structure: Breast cancer, lobular OMIM:[192090], Cleft lip with or without cleft palate, with gastric cancer, familial diffuse OMIM:[192090], Endometrial carcinoma OMIM:[192090], Gastric cancer, familial diffuse OMIM:[192090], Listeria monocytogenes, susceptibility to OMIM:[192090], Ovarian carcinoma OMIM:[192090]
About this Structure
1O6S is a Protein complex structure of sequences from Homo sapiens and Listeria monocytogenes with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin., Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW, Cell. 2002 Dec 13;111(6):825-36. PMID:12526809
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