1p7h
From Proteopedia
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| - | [[Image:1p7h.gif|left|200px]] | + | [[Image:1p7h.gif|left|200px]] |
| - | + | ||
| - | '''Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element''' | + | {{Structure |
| + | |PDB= 1p7h |SIZE=350|CAPTION= <scene name='initialview01'>1p7h</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= NFATC2 OR NFAT1 OR NFATP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P7H is a [ | + | 1P7H is a [[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=1P7H OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element., Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L, Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:[http:// | + | Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element., Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L, Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12949493 12949493] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:54 2008'' |
Revision as of 11:20, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | NFATC2 OR NFAT1 OR NFATP (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element
Overview
DNA binding by NFAT1 as a dimer has been implicated in the activation of host and viral genes. Here we report a crystal structure of NFAT1 bound cooperatively as a dimer to the highly conserved kappa B site from the human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR). This structure reveals a new mode of dimerization and protein-DNA recognition by the Rel homology region (RHR) of NFAT1. The two NFAT1 monomers form a complete circle around the kappa B DNA through protein-protein interactions mediated by both their N- and C-terminal subdomains. The major dimer interface, formed by the C-terminal domain, is asymmetric and substantially different from the symmetric dimer interface seen in other Rel family proteins. Comparison to other NFAT structures, including NFAT5 and the NFAT1-Fos-Jun-ARRE2 complex, reveals that NFAT1 adopts different conformations and its protein surfaces mediate distinct protein-protein interactions in the context of different DNA sites.
About this Structure
1P7H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element., Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L, Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:12949493
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