1o6s
From Proteopedia
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|PDB= 1o6s |SIZE=350|CAPTION= <scene name='initialview01'>1o6s</scene>, resolution 1.80Å | |PDB= 1o6s |SIZE=350|CAPTION= <scene name='initialview01'>1o6s</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6s OCA], [http://www.ebi.ac.uk/pdbsum/1o6s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o6s RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Breast cancer, lobular OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]], Cleft lip with or without cleft palate, with gastric cancer, familial diffuse OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]], Endometrial carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]], Gastric cancer, familial diffuse OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]], Listeria monocytogenes, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]], Ovarian carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192090 192090]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Wehland, J.]] | [[Category: Wehland, J.]] | ||
[[Category: Ziehm, T.]] | [[Category: Ziehm, T.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
[[Category: bacterial infection]] | [[Category: bacterial infection]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
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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 Sun Mar 30 22:40:42 2008'' |
Revision as of 19:40, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTERNALIN (LISTERIA MONOCYTOGENES) / E-CADHERIN (HUMAN) RECOGNITION COMPLEX
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.
About this Structure
1O6S is a Protein complex structure of sequences from Homo sapiens and Listeria monocytogenes. 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
Page seeded by OCA on Sun Mar 30 22:40:42 2008
