Sandbox Reserved 816: Difference between revisions
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Lecomte Alix (talk | contribs) No edit summary |
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== Introduction == | ==== Introduction ==== | ||
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'''Internalin K''' is involved in [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] ability to escape from autophagy by recruitment of [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein] to the bacterial surface. | '''Internalin K''' is involved in [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] ability to escape from autophagy by recruitment of [http://en.wikipedia.org/wiki/Major_vault_protein major vault protein] to the bacterial surface. | ||
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====Structure of Internalin K==== | |||
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== Internalin family's generalities == | |||
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'''L.monocytogenes''' uses a lot of virulence factors to initiate infection. Proteins of the '''internalin's family''', virulence factors, plays a key role in the infection's survival in a variety of cell types. They play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. The internalin family uses a binding partner action. | |||
'''The three-dimensional structure''' of the internalin family shows that there are modular proteins in order to improve the binding's partner. A common architecture is pointed, the N-terminal domain, also called N-terminal '''leucine-rich repeats''' (LRRs). It is composed of 22-residue regions including a β-strand and an helix. The structure is a curved solenoid. '''LRR''' is followed by domains in cell signaling and often in bacterial surface attachment. Whereas the C-terminal regions are not similar that contributes the variety of roles. Each internalin plays a specific role in the infection. | |||
== '''Structure of Internalin K''' == | |||