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Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex.

Nolte RT, Conlin RM, Harrison SC, Brown RS
Proc Natl Acad Sci U S A 95 2938-43 (1998)
Cited: 129 times
EuropePMC logo PMID: 9501194

Abstract

The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 bp of the 5S rRNA gene promoter has been determined at 3.1 A resolution. Individual zinc fingers are positioned differently in the major groove and across the minor groove of DNA to span the entire length of the duplex. These results show how TFIIIA can recognize several separated DNA sequences by using fewer fingers than necessary for continuous winding in the major groove.

Reviews - 1tf6 mentioned but not cited (2)

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Articles - 1tf6 mentioned but not cited (8)

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  8. Letter Native, sequential protein folding via anchored N and C protein termini. Alberti S. Proc Natl Acad Sci U S A 113 E3189-91 (2016)


Reviews citing this publication (32)

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