Sandbox Reserved 816: Difference between revisions
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Structural comparison of the regions that follow the LRR domains in Internalin K (yellow) shows that Internalin K has a more complex fold. | Structural comparison of the regions that follow the LRR domains in Internalin K (yellow) shows that Internalin K has a more complex fold. | ||
==== '''Structure of Internalin K''' ==== | ==== '''Structure of Internalin K''' ==== | ||
[[Image: | [[Image:Chain2.png | right]] | ||
'''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''. | '''Internalin K''' is a multi-domain virulence factor. It harbours four domains formed in the shape of '''"bent arm"'''. | ||
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<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. | <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. | ||
