Sandbox Reserved 816: Difference between revisions
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=='''Introduction'''== | =='''Introduction'''== | ||
'''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] | '''Internalin K''' is a protein from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] which is a [http://en.wikipedia.org/wiki/Gram-positive_bacteria Gram-positive bacterium] human pathogen. Its the ability to survive in the human intestine and to cross a variety of membranes, including mucosal, intestinal, placental, and blood–brain barriers, allows it to generate illnesses ranging from gastroenteritis in healthy individuals to bacteremia and meningitis in immunocompromised patients, as well as mother-to-child infections.These pathologies are caused by the unusual capacity of the bacterium to cross three host barriers during infection and to invade nonphagocytic cells. [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogene] can survive in a variety of cell types and proteins of the internalin family have been shown to play a key role in this survival | ||
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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 | '''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 there are 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 | '''The three-dimensional structure''' of the internalin family shows that there are modular proteins in order to improve the link with the 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. | ||
[[Image:Internalin.jpg]] | [[Image:Internalin.jpg]] | ||
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[[Image:Internalin K.jpg]] | [[Image:Internalin K.jpg]] | ||
<scene name='56/568014/D1/1'>D1</scene> and <scene name='56/568014/D2/1'>D2</scene> are involved in binding to protein partners while <scene name='56/568014/D3/1'>D3</scene> and <scene name='56/568014/D4/1'>D4</scene> most probably serve as pedestals. The flexibility between domains of its elongated structure may play a key role in this complex function. | |||