Published in Blood Weekly, October 14th, 2004
According to published research from the United States, "The human cytomegalovirus DNA polymerase consists of a catalytic subunit, UL54, and a presumed processivity factor, UL44. We have solved the crystal structure of residues 1-290 of UL44 to 1.85 Angstrom resolution by multiwavelength anomalous dispersion."
"The structure reveals a dimer of UL44 in the shape of a C clamp. Each monomer of UL44 shares its overall fold with other processivity factors, including herpes simplex virus UL42, which is a monomer that binds DNA directly, and the sliding clamp, PCNA, which is a...
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Source: Blood Weekly (2004-10-14)
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