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1zfd

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[[Image:1zfd.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1zfd", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1zfd| PDB=1zfd | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfd OCA], [http://www.ebi.ac.uk/pdbsum/1zfd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zfd RCSB]</span>
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'''SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES'''
'''SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES'''
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[[Category: Rhodes, D.]]
[[Category: Rhodes, D.]]
[[Category: Schwabe, J W.R.]]
[[Category: Schwabe, J W.R.]]
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[[Category: dna binding motif]]
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[[Category: Dna binding motif]]
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[[Category: zinc finger dna binding domain]]
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[[Category: Zinc finger dna binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:33:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:35:15 2008''
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Revision as of 14:33, 3 May 2008

Template:STRUCTURE 1zfd

SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES


Overview

This paper describes the detailed three-dimensional structures of two zinc-finger domains from the yeast transcription factor SWI5, calculated using the results of the n.m.r. experiments described in the accompanying paper. The structure of finger 2 is essentially similar to those previously obtained by others for isolated, synthetic single zinc-finger domains in solution, and for the three zinc-finger peptide Zif268 in its crystalline complex with DNA. The N-terminal half of the sequence forms a two-stranded, irregular beta-sheet containing both of the metal-binding cysteine residues, while the remainder of the structure forms a helix. Approximately the first half of this helix is alpha-helical, whereas the C-terminal portion, including the two metal-binding histidine residues, is 3(10) helical. Four invariant hydrophobic residues form a core to the structure. In contrast to all previously described structures of zinc-finger domains, finger 1 has an additional strand in the beta-sheet, formed by residues N-terminal to the formal start of the finger motif. This additional strand plays a role in stabilising the folded form of finger 1, since a two-finger peptide lacking the N-terminal residues showed folded structure in finger 2 but not in finger 1.

About this Structure

1ZFD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet., Neuhaus D, Nakaseko Y, Schwabe JW, Klug A, J Mol Biol. 1992 Nov 20;228(2):637-51. PMID:1453468 Page seeded by OCA on Sat May 3 17:33:22 2008

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