Literature summary for 3.1.26.13 extracted from

Jones, F.D.; Hughes, S.H.
In vitro analysis of the effects of mutations in the G-tract of the human immunodeficiency virus type 1 polypurine tract on RNase H cleavage specificity (2007), Virology, 360, 341-349.

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Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the recognition and precise cleavage of the polypurine tract of the human immunodeficiency virus type 1 is an essential step in HIV-1 reverse transcription. Mutations at positions 2 and 5 of the 3'-end of the polypurine tract do significantly alter the cleavage specificity at the polypurine tract/U3 junction. The structure of the polypurine tract primer, rather than the base-specific contacts between the polypurine tract and HIV-1 RT, are the primary determinants of RNase H cleavage specificity at the polypurine tract/U3 junction	Human immunodeficiency virus 1	?	-	?

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Release 2023.1 (January 2023)