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Design, synthesis and structure of a zinc finger with an artificial beta-turn.
Viles, J H; Patel, S U; Mitchell, J B; Moody, C M; Justice, D E; Uppenbrink, J; Doyle, P M; Harris, C J; Sadler, P J; Thornton, J M.
Afiliación
  • Viles JH; Department of Chemistry, Birkbeck College, University of London, Gordon House, London, WC1H 0PP, UK.
J Mol Biol ; 279(4): 973-86, 1998 Jun 19.
Article en En | MEDLINE | ID: mdl-9642075
We have incorporated a bicyclic beta-turn mimetic (BTD; beta-turn dipeptide) into a zinc finger, creating a zinc finger with an artificial beta-turn. The designed peptide chelates zinc and has the same fold as the unmodified native zinc finger (finger 3 of the human YY1 protein). A combination of 1H NMR and structure calculations reveals that, in solution, this zinc finger has a fold similar to the known wild-type crystal structure and to other zinc fingers containing the consensus sequence X3-Cys-X4-Cys-X12-His-X3-His-X. The peptide was designed with BTD between the chelating cysteine residues, with BTD forming a type II' beta-turn linking the two strands of a distorted anti-parallel beta-sheet. The C-terminal portion of the peptide forms a helix with zinc co-ordinating histidine residues on successive turns of the helix. This work represents a step towards developing methods by which parts of a target protein may be replaced by peptide mimetics.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Diseño de Fármacos / Dedos de Zinc Límite: Humans Idioma: En Revista: J Mol Biol Año: 1998 Tipo del documento: Article Pais de publicación: Países Bajos
Buscar en Google
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Diseño de Fármacos / Dedos de Zinc Límite: Humans Idioma: En Revista: J Mol Biol Año: 1998 Tipo del documento: Article Pais de publicación: Países Bajos