1ZNM

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

Summary for 1ZNM

• Entry DOI: 10.2210/pdb1znm/pdb
• Descriptor: YY1, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, zn-btd(7, 8)-3yy1, beta-turn mimetic, transcription regulation
• Cellular location: Nucleus matrix : P25490
• Total number of polymer chains: 1
• Total formula weight: 3299.24

Authors

Viles, J.H.,Patel, S.U.,Mitchell, J.B.O.,Moody, C.M.,Justice, D.E.,Uppenbrink, J.,Doyle, P.M.,Harris, C.J.,Sadler, P.J.,Thornton, J.M. (deposition date: 1997-11-20, release date: 1998-04-01, Last modification date: 2024-10-23)

Primary citation

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.
Design, synthesis and structure of a zinc finger with an artificial beta-turn.
J.Mol.Biol., 279:973-986, 1998

PubMed Abstract: 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.

PubMed: 9642075
DOI: 10.1006/jmbi.1998.1764

Experimental method

SOLUTION NMR