1d0b
From Proteopedia
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'''INTERNALIN B LEUCINE RICH REPEAT DOMAIN''' | '''INTERNALIN B LEUCINE RICH REPEAT DOMAIN''' | ||
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[[Category: Ghosh, P.]] | [[Category: Ghosh, P.]] | ||
[[Category: Marino, M.]] | [[Category: Marino, M.]] | ||
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- | [[Category: | + | [[Category: Leucine rich repeat]] |
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Revision as of 10:18, 2 May 2008
INTERNALIN B LEUCINE RICH REPEAT DOMAIN
Overview
The L. monocytogenes protein lnlB activates phosphoinositide 3-kinase and induces phagocytosis in several mammalian cell types. The 1.86 A resolution X-ray crystal structure of the leucine-rich repeat domain of lnlB that is both necessary and sufficient to induce phagocytosis is presented here. The structure supports a crucial role for calcium in host cell invasion by L. monocytogenes and supplies a rationale for its function. Calciums are bound to the protein in an unusually exposed manner that suggests that the metals may act as a bridge between lnlB and mammalian cell surface receptors. The structure also identifies surfaces on the curved and elongated molecule that may constitute additional interaction sites in forming a bacterial-mammalian signaling complex.
About this Structure
1D0B is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes., Marino M, Braun L, Cossart P, Ghosh P, Mol Cell. 1999 Dec;4(6):1063-72. PMID:10635330 Page seeded by OCA on Fri May 2 13:18:06 2008