1pzu

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(New page: 200px<br /> <applet load="1pzu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pzu, resolution 3.10&Aring;" /> '''An asymmetric NFAT1...)
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[[Image:1pzu.gif|left|200px]]<br />
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[[Image:1pzu.gif|left|200px]]<br /><applet load="1pzu" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1pzu" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1pzu, resolution 3.10&Aring;" />
caption="1pzu, resolution 3.10&Aring;" />
'''An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site'''<br />
'''An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site'''<br />
==Overview==
==Overview==
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The crystal structure of the NFAT1 Rel homology region (RHR) bound to a, pseudo-palindromic DNA site reveals an asymmetric dimer interaction, between the RHR-C domains, unrelated to the contact seen in Rel dimers, such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective, in the dimer contact show loss of cooperativity and demonstrate that the, same interaction is present in solution. The structure we have determined, may correspond to a functional NFAT binding mode at palindromic sites of, genes induced during the anergic response to weak TCR signaling.
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The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.
==About this Structure==
==About this Structure==
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1PZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PZU OCA].
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1PZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZU OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, L.]]
[[Category: Chen, L.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
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[[Category: Hogan, P.G.]]
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[[Category: Hogan, P G.]]
[[Category: Jin, L.]]
[[Category: Jin, L.]]
[[Category: Macian, F.]]
[[Category: Macian, F.]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:48:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:20 2008''

Revision as of 12:34, 21 February 2008


1pzu, resolution 3.10Å

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An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site

Overview

The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.

About this Structure

1PZU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

An asymmetric NFAT1 dimer on a pseudo-palindromic kappa B-like DNA site., Jin L, Sliz P, Chen L, Macian F, Rao A, Hogan PG, Harrison SC, Nat Struct Biol. 2003 Oct;10(10):807-11. Epub 2003 Aug 31. PMID:12949491

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