1o6v: Difference between revisions
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[[Image:1o6v.gif|left|200px]]<br /><applet load="1o6v" size=" | [[Image:1o6v.gif|left|200px]]<br /><applet load="1o6v" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1o6v, resolution 1.50Å" /> | caption="1o6v, resolution 1.50Å" /> | ||
'''INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN UNCOMPLEXED'''<br /> | '''INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN UNCOMPLEXED'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1O6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 1O6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: leucine rich repeat]] | [[Category: leucine rich repeat]] | ||
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Revision as of 10:54, 3 February 2008
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INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN UNCOMPLEXED
OverviewOverview
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 StructureAbout this Structure
1O6V is a Single protein structure of sequence from Listeria monocytogenes with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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