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Title: Structure of Aart, a Designed Six-finger Zinc Finger Peptide, Bound to DNA

Authors:
; ; ; ;  [1];  [2];  [2]
  1. (UCD)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Science Foundation (NSF)
OSTI Identifier:
1222842
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Mol. Biol.; Journal Volume: 363; Journal Issue: (2) ; 10, 2006
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Segal, David J., Crotty, Justin W., Bhakta, Mital S., Barbas, III, Carlos F., Horton, Nancy C., Scripps), and Ariz). Structure of Aart, a Designed Six-finger Zinc Finger Peptide, Bound to DNA. United States: N. p., 2016. Web. doi:10.1016/j.jmb.2006.08.016.
Segal, David J., Crotty, Justin W., Bhakta, Mital S., Barbas, III, Carlos F., Horton, Nancy C., Scripps), & Ariz). Structure of Aart, a Designed Six-finger Zinc Finger Peptide, Bound to DNA. United States. doi:10.1016/j.jmb.2006.08.016.
Segal, David J., Crotty, Justin W., Bhakta, Mital S., Barbas, III, Carlos F., Horton, Nancy C., Scripps), and Ariz). Tue . "Structure of Aart, a Designed Six-finger Zinc Finger Peptide, Bound to DNA". United States. doi:10.1016/j.jmb.2006.08.016.
@article{osti_1222842,
title = {Structure of Aart, a Designed Six-finger Zinc Finger Peptide, Bound to DNA},
author = {Segal, David J. and Crotty, Justin W. and Bhakta, Mital S. and Barbas, III, Carlos F. and Horton, Nancy C. and Scripps) and Ariz)},
abstractNote = {},
doi = {10.1016/j.jmb.2006.08.016},
journal = {J. Mol. Biol.},
number = (2) ; 10, 2006,
volume = 363,
place = {United States},
year = {Tue Jul 05 00:00:00 EDT 2016},
month = {Tue Jul 05 00:00:00 EDT 2016}
}
  • No abstract prepared.
  • No abstract prepared.
  • Preliminary data analysis of crystals of a designed six-finger zinc-finger protein bound to DNA is presented. The cell likely contains two protein–DNA complexes and diffracts to 2.95 Å. Crystals of a designed six-finger zinc-finger protein, Aart, bound to a 22-base-pair duplex DNA containing a consensus binding site have been obtained. Crystals grew by hanging-drop vapor diffusion from solutions containing polyethylene glycol 4000 as the precipitating agent. The irregularly shaped crystals belong to space group P1, with unit-cell parameters a = 41.95, b = 71.76, c = 74.73 Å, α = 100.87, β = 96.22, γ = 106.33°. There are mostmore » likely to be two protein–DNA complexes in the asymmetric unit. A complete native data set has been collected from a high-energy synchrotron source to a resolution of 2.95 Å at 100 K, with an R{sub merge} of 9.3%.« less
  • No abstract prepared.
  • The addition of a new function to native proteins is one of the most attractive protein-based designs. In this study, we have converted a C{sub 2}H{sub 2}-type zinc finger as a DNA-binding motif into a novel zinc finger-type nuclease by connecting two distinct zinc finger proteins (Sp1 and GLI) with a functional linker possessing DNA cleavage activity. As a DNA cleavage domain, we chose an analogue of the metal-binding loop (12 amino acid residues), peptide P1, which has been reported to exhibit a strong binding affinity for a lanthanide ion and DNA cleavage ability in the presence of Ce(IV). Ourmore » newly designed nucleases, Sp1(P1)GLI and Sp1(P1G)GLI, can strongly bind to a lanthanide ion and show a unique DNA cleavage pattern, in which certain positions between the two DNA-binding sites are specifically cleaved. The present result provides useful information for expanding the design strategy for artificial nucleases.« less