1znm
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A ZINC FINGER WITH AN ARTIFICIAL BETA-TURN, ORIGINAL SEQUENCE TAKEN FROM THE THIRD ZINC FINGER DOMAIN OF THE HUMAN TRANSCRIPTIONAL REPRESSOR PROTEIN YY1 (YING AND YANG 1, A DELTA TRANSCRIPTION FACTOR), NMR, 34 STRUCTURES
Overview
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.
About this Structure
1ZNM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Design, synthesis and structure of a zinc finger with an artificial beta-turn., Viles JH, Patel SU, Mitchell JB, Moody CM, Justice DE, Uppenbrink J, Doyle PM, Harris CJ, Sadler PJ, Thornton JM, J Mol Biol. 1998 Jun 19;279(4):973-86. PMID:9642075
Page seeded by OCA on Sun Mar 23 14:30:11 2008
