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1pxe

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(New page: 200px<br /><applet load="1pxe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pxe" /> '''Solution Structure of a CCHHC Domain of Neur...)
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'''Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1'''<br />
'''Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1'''<br />
==Overview==
==Overview==
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The structure of a CCHHC zinc-binding domain from neural zinc finger, factor-1 (NZF-1) has been determined in solution though the use of NMR, methods. This domain is a member of a family of domains that have the, Cys-X(4)-Cys-X(4)-His-X(7)-His-X(5)-Cys consensus sequence. The structure, determination reveals a novel fold based around a zinc(II) ion coordinated, to three Cys residues and the second of the two conserved His residues., The other His residue is stacked between the metal-coordinated His residue, and a relatively conserved aromatic residue. Analysis of His to Gln, sequence variants reveals that both His residues are required for the, formation of a well-defined structure, but neither is required for, high-affinity metal binding at a tetrahedral site. The structure suggests, that a two-domain protein fragment and a double-stranded DNA binding site, may interact with a common two-fold axis relating the two domains and the, two half-sites of the DNA-inverted repeat.
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The structure of a CCHHC zinc-binding domain from neural zinc finger factor-1 (NZF-1) has been determined in solution though the use of NMR methods. This domain is a member of a family of domains that have the Cys-X(4)-Cys-X(4)-His-X(7)-His-X(5)-Cys consensus sequence. The structure determination reveals a novel fold based around a zinc(II) ion coordinated to three Cys residues and the second of the two conserved His residues. The other His residue is stacked between the metal-coordinated His residue and a relatively conserved aromatic residue. Analysis of His to Gln sequence variants reveals that both His residues are required for the formation of a well-defined structure, but neither is required for high-affinity metal binding at a tetrahedral site. The structure suggests that a two-domain protein fragment and a double-stranded DNA binding site may interact with a common two-fold axis relating the two domains and the two half-sites of the DNA-inverted repeat.
==About this Structure==
==About this Structure==
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1PXE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PXE OCA].
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1PXE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXE OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Amann, B.T.]]
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[[Category: Amann, B T.]]
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[[Category: Berg, J.M.]]
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[[Category: Berg, J M.]]
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[[Category: Berkovits-Cymet, H.J.]]
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[[Category: Berkovits-Cymet, H J.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: cchhc zinc binding domain]]
[[Category: cchhc zinc binding domain]]
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[[Category: neural zinc finger factor-1]]
[[Category: neural zinc finger factor-1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:12:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:41 2008''

Revision as of 12:33, 21 February 2008


1pxe

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Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1

Overview

The structure of a CCHHC zinc-binding domain from neural zinc finger factor-1 (NZF-1) has been determined in solution though the use of NMR methods. This domain is a member of a family of domains that have the Cys-X(4)-Cys-X(4)-His-X(7)-His-X(5)-Cys consensus sequence. The structure determination reveals a novel fold based around a zinc(II) ion coordinated to three Cys residues and the second of the two conserved His residues. The other His residue is stacked between the metal-coordinated His residue and a relatively conserved aromatic residue. Analysis of His to Gln sequence variants reveals that both His residues are required for the formation of a well-defined structure, but neither is required for high-affinity metal binding at a tetrahedral site. The structure suggests that a two-domain protein fragment and a double-stranded DNA binding site may interact with a common two-fold axis relating the two domains and the two half-sites of the DNA-inverted repeat.

About this Structure

1PXE is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of a CCHHC domain of neural zinc finger factor-1 and its implications for DNA binding., Berkovits-Cymet HJ, Amann BT, Berg JM, Biochemistry. 2004 Feb 3;43(4):898-903. PMID:14744132

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