Sandbox Reserved 1739: Difference between revisions
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The relevance of Hepatitis C helicase/primase is that the helicase/protease combination in HCV is believed to play a pivotal role in the replication cycle of HCV. The helicase exists as a dimer, bearing mutations, and can be found in three different functional states (9). The three functional states include a substrate-unbound state, an ATP-bound state, and an NA-bound state. The presence of ATP transitions the protease from high NA binding affinity to low NA binding affinity. The cooperation of helicase/protease binding the DNA is affected by the length of the ss lattice, and the desired ss DNA length is around 22nt (3). | The relevance of Hepatitis C helicase/primase is that the helicase/protease combination in HCV is believed to play a pivotal role in the replication cycle of HCV. The helicase exists as a dimer, bearing mutations, and can be found in three different functional states (9). The three functional states include a substrate-unbound state, an ATP-bound state, and an NA-bound state. The presence of ATP transitions the protease from high NA binding affinity to low NA binding affinity. The cooperation of helicase/protease binding the DNA is affected by the length of the ss lattice, and the desired ss DNA length is around 22nt (3). | ||
== Structural highlights == | == Structural highlights == | ||
<scene name='91/919048/2OBQ/1'>2OBQ</scene> | <scene name='91/919048/2OBQ/1'>2OBQ for Hepatitis primase:</scene> | ||
Method: X-Ray Diffraction. | Method: X-Ray Diffraction. | ||
Resolution: 2.50 Å. | Resolution: 2.50 Å. | ||
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<scene name='91/919048/Hepatitis_c_helicase/1'> | <scene name='91/919048/Hepatitis_c_helicase/1'> | ||
8OHM for Hepatitis helicase: | 8OHM for Hepatitis helicase:</scene> | ||
Method: X-Ray Diffraction. | Method: X-Ray Diffraction. | ||
Resolution: 2.30 Å. | Resolution: 2.30 Å. | ||
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Secondary Structure: beta sheets sandwiched between Alpha helices. | Secondary Structure: beta sheets sandwiched between Alpha helices. | ||
Tertiary Structure: alpha helices + beta sheets. Domains: 3 domains; domain 2 is linked to domains 1 and 3 by flexible linkers. Motifs present: 6 motifs; the Walker A motif, the Phe loop, and the Arg-clamp motif (14). | Tertiary Structure: alpha helices + beta sheets. Domains: 3 domains; domain 2 is linked to domains 1 and 3 by flexible linkers. Motifs present: 6 motifs; the Walker A motif, the Phe loop, and the Arg-clamp motif (14). | ||
== References == | == References == | ||
