The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.

Y. Hori, K. Suzuki, Y. Okuno, M. Nagaoka, S. Futaki, Y. Sugiura

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

We have created a novel His4-type zinc finger protein (H4Sp1) engineered by Cys-->His mutations of the Cys2His2-type zinc finger in transcription factor Sp1. The CD and NMR studies reveal that the His4 domain has Zn(II)-dependent folding properties and similar secondary structures to wild-type Cys2His2 domain. The DNA binding experiments demonstrate that H4Sp1 can bind DNA in a specific way. The present artificial peptide H4Sp1 will provide valuable information about the interaction between a metallopeptide and DNA.

Original languageEnglish
Pages (from-to)295-296
Number of pages2
JournalNucleic acids symposium series
Issue number44
DOIs
Publication statusPublished - 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Medicine(all)

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