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From Proteopedia
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== UvrD == | == UvrD == | ||
UvrD, also known as Helicase II, is one of many components responsible in repairing DNA damage. UvrD is involved in nucleotide excision repair (NER) and transcription-coupled DNA repair (TCR repair). TCR repair occurs during transcription when Helicase II binds to a RNA polymerase (RNAP) and slides backwards in order to fix the mismatched nucleotide. One of the main structural components of how UvrD binds to RNAP is by having a Tudor-domain like fold. This helps better explain the UvrD-RNAP interaction, which is a better explanation than just having nucleic-acid affinity. A main cause in damage to DNA, which requires for nucleotide excision repair is from UV radiation, which can come from multiple sources, including sunlight and UV light from tanning beds. | UvrD, also known as Helicase II, is one of many components responsible in repairing DNA damage. UvrD is involved in nucleotide excision repair (NER) and transcription-coupled DNA repair (TCR repair). TCR repair occurs during transcription when Helicase II binds to a RNA polymerase (RNAP) and slides backwards in order to fix the mismatched nucleotide. One of the main structural components of how UvrD binds to RNAP is by having a Tudor-domain like fold. This helps better explain the UvrD-RNAP interaction, which is a better explanation than just having nucleic-acid affinity. A main cause in damage to DNA, which requires for nucleotide excision repair is from UV radiation, which can come from multiple sources, including sunlight and UV light from tanning beds. | ||
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== UvrD Binding Site for DNA == | == UvrD Binding Site for DNA == | ||
Revision as of 03:07, 4 October 2022
Contents |
DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX
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UvrD
UvrD, also known as Helicase II, is one of many components responsible in repairing DNA damage. UvrD is involved in nucleotide excision repair (NER) and transcription-coupled DNA repair (TCR repair). TCR repair occurs during transcription when Helicase II binds to a RNA polymerase (RNAP) and slides backwards in order to fix the mismatched nucleotide. One of the main structural components of how UvrD binds to RNAP is by having a Tudor-domain like fold. This helps better explain the UvrD-RNAP interaction, which is a better explanation than just having nucleic-acid affinity. A main cause in damage to DNA, which requires for nucleotide excision repair is from UV radiation, which can come from multiple sources, including sunlight and UV light from tanning beds. load='2IS4'
