1sp2

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(New page: 200px<br /> <applet load="1sp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sp2" /> '''NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM ...)
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==About this Structure==
==About this Structure==
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1SP2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] 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=1SP2 OCA]].
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1SP2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: S1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SP2 OCA]].
==Reference==
==Reference==
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:09:11 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:29:48 2007''

Revision as of 06:25, 30 October 2007


1sp2

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NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F2, MINIMIZED AVERAGE STRUCTURE

Overview

The carboxyl terminus of transcription factor Sp1 contains three, contiguous Cys2-His2 zinc finger domains with the consensus sequence, Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear, two-dimensional NMR techniques to solve the solution structures of, synthetic peptides corresponding to the last two zinc finger domains, (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical, Cys2-His2 type fold for both the domains differing from each other, primarily in the conformation of Cys-X2-Cys (beta-type I turn) and, Cys-X4-Cys (beta-type II turn) elements. There are, however, no, significant differences in the metal binding properties between the, Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The, free solution structures of Sp1f2 and ... [(full description)]

About this Structure

1SP2 is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

Reference

Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition., Narayan VA, Kriwacki RW, Caradonna JP, J Biol Chem. 1997 Mar 21;272(12):7801-9. PMID:9065444

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