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An expanded binding model for Cys2His2 zinc finger protein-DNA interfaces.

ABSTRACT: Cys(2)His(2) zinc finger (C2H2-ZF) proteins comprise the largest class of eukaryotic transcription factors. The 'canonical model' for C2H2-ZF protein-DNA interaction consists of only four amino acid-nucleotide contacts per zinc finger domain, and this model has been the basis for several efforts for computationally predicting and experimentally designing protein-DNA interfaces. Here, we perform a systematic analysis of structural and experimental binding data and find that, in addition to the canonical contacts, several other amino acid and base pair combinations frequently play a role in C2H2-ZF protein-DNA binding. We suggest an expansion of the canonical C2H2-ZF model to include one to three additional contacts, and show that computational approaches including these additional contacts improve predictions of DNA targets of zinc finger proteins.

SUBMITTER: Persikov AV

PROVIDER: S-EPMC3402046 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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An expanded binding model for Cys2His2 zinc finger protein-DNA interfaces.

Persikov Anton V AV Singh Mona M

Physical biology 20110513 3

Cys(2)His(2) zinc finger (C2H2-ZF) proteins comprise the largest class of eukaryotic transcription factors. The 'canonical model' for C2H2-ZF protein-DNA interaction consists of only four amino acid-nucleotide contacts per zinc finger domain, and this model has been the basis for several efforts for computationally predicting and experimentally designing protein-DNA interfaces. Here, we perform a systematic analysis of structural and experimental binding data and find that, in addition to the ca ...[more]

PMID: 21572177

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| S-EPMC4053984 | biostudies-literature

The geometric influence on the Cys2His2 zinc finger domain and functional plasticity.

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| S-EPMC7293014 | biostudies-literature

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