1znm
From Proteopedia
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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''' | '''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''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZNM is a [[Single protein]] structure | + | 1ZNM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Uppenbrink, J.]] | [[Category: Uppenbrink, J.]] | ||
[[Category: Viles, J H.]] | [[Category: Viles, J H.]] | ||
| - | [[Category: | + | [[Category: Beta-turn mimetic]] |
| - | + | [[Category: Transcription regulation]] | |
| - | [[Category: | + | [[Category: Zinc finger]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:50:58 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:50, 3 May 2008
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. 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 Sat May 3 17:50:58 2008
