1znm

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==Overview==
==Overview==
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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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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==
==About this Structure==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9642075 9642075]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9642075 9642075]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Doyle, P.M.]]
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[[Category: Doyle, P M.]]
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[[Category: Harris, C.J.]]
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[[Category: Harris, C J.]]
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[[Category: Justice, D.E.]]
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[[Category: Justice, D E.]]
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[[Category: Mitchell, J.B.O.]]
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[[Category: Mitchell, J B.O.]]
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[[Category: Moody, C.M.]]
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[[Category: Moody, C M.]]
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[[Category: Patel, S.U.]]
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[[Category: Patel, S U.]]
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[[Category: Sadler, P.J.]]
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[[Category: Sadler, P J.]]
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[[Category: Thornton, J.M.]]
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[[Category: Thornton, J M.]]
[[Category: Uppenbrink, J.]]
[[Category: Uppenbrink, J.]]
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[[Category: Viles, J.H.]]
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[[Category: Viles, J H.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: 8)-3yy1]]
[[Category: 8)-3yy1]]
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[[Category: zn-btd(7]]
[[Category: zn-btd(7]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:22:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:20 2008''

Revision as of 14:17, 21 February 2008


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] with as ligand. Known structural/functional Sites: and . 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

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