This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
The function of Hepatitis C primase is to build the viral capsid. The viral capsid and two glycoproteins make up the genome (1).
The function of Hepatitis C helicase is to stop viral RNA from binding by stripping it of its proteins. It is necessary for viral replication (2). Helicase can process a wide range of nucleic acid sequences and unwind them (5).
Together, Hepatitis C primase and helicase function to ----
Disease
Hepatitis C (HCV) is a viral infection that causes inflammation of the liver. As of 2022 there has been no vaccine created for Hepatitis C (6).
Relevance
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
2OBQ: for Hepatisis primase
Method: X-Ray Diffraction.
Resolution: 2.50 Å.
Classification: Viral Protein.
Organism(s): Hepacivirus C.
Expression System: Escherichia coli.
Deposited: 2006-12-19.
Released: 2007-07-31.
Deposition Author(s): Prongay, A.J., Guo, Z., Yao, N., Fischmann, T., Strickland, C., Myers Jr., J., Weber, P.C., Malcolm, B., Beyer, B.M., Ingram, R., Pichardo, J., Hong, Z., Prosise, W.W., Ramanathan, L., Taremi, S.S., Yarosh-Tomaine, T., Zhang, R., Senior, M., Yang, R., Arasappan, A., Bennett, F., Bogen, S.F., Chen, K., Jao, E., Liu, Y., Love, R.G., Saksena, A.K., Venkatraman, S., Girijavallabhan, V., Njoroge, F.G., Madison, V.
Primary Structure: 180 amino acids.
Secondary Structure (what types of secondary structure in the protein and number of each):
Tertiary Structure(motif(s) present, domains):
Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry):
8OHM for Hepatitis helicase:
Method: X-Ray Diffraction.
Resolution: 2.30 Å.
Classification: Helicase.
Organism(s): Hepacivirus C.
Expression System: Escherichia coli BL21(DE3).
Deposited: 1998-03-13.
Released: 1999-04-20.
Deposition Author(s): Cho, H.S., Ha, N.C., Kang, L.W., Oh, B.H.
Primary Structure: 620 amino acids.
Secondary Structure (what types of secondary structure in the protein and number of each): Beta sheets sandwiched between Alpha helices.
Tertiary Structure(motif(s) present, domains):
Quaternary Structure(number of subunits, quaternary structure name, quaternary symmetry):
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.