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1irg

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{{STRUCTURE_1irg| PDB=1irg | SCENE= }}
{{STRUCTURE_1irg| PDB=1irg | SCENE= }}
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'''INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, 20 STRUCTURES'''
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===INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, 20 STRUCTURES===
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==Overview==
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BACKGROUND: The transcription of interferon (IFN) and IFN-inducible genes is mainly regulated by the interferon regulatory factor (IRF) family of proteins, which recognize a unique AAGTGA hexamer repeat motif in the regulatory region of IFN genes. A DNA-binding domain of approximately 100 amino acids has been commonly found in the IRF family of proteins, but it has no sequence homology to known DNA-binding motifs. Elucidation of the structures of members of the IRF family is therefore useful to the understanding of the regulation and evolution of the immune system at the structural level. RESULTS: The solution structure of the DNA-binding domain of interferon regulatory factor-2 (IRF-2) has been determined by NMR spectroscopy. It is composed of a four-stranded antiparallel beta sheet and three alpha helices, and its global fold is similar to those of the winged helix-turn-helix (wHTH) family of proteins. A long loop (Pro37-Asp51) is found immediately before the HTH motif, which is not found in other wHTH proteins. The NMR signals of residues in this long loop, as well as the second helix of the HTH motif, are strongly affected upon the addition of the hexamer repeat DNA, suggesting that these structural elements participate in DNA recognition and binding. CONCLUSIONS: The structural similarity of the DNA-binding domain of IRF-2 with those of proteins in the wHTH family shows that the IRF proteins belong to the wHTH family, even though there is no apparent sequence homology among proteins of the two families. The sequential structure alignment program (SSAP) shows that IRF-2 has a slightly different structure from typical wHTH proteins, mainly in the orientation of helix 2. The IRF family of proteins should therefore be categorized into a subfamily of the wHTH family. The evidence here implies that the evolutional pathway of the IRF family is distinct from that of the other wHTH proteins, in other words, the immune system diverged from an evolutional stem at an early stage.
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{{ABSTRACT_PUBMED_9562558}}
==About this Structure==
==About this Structure==
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1IRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRG OCA].
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1IRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRG OCA].
==Reference==
==Reference==
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[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Winged helix-turn-helix]]
[[Category: Winged helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:19:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:52:12 2008''

Revision as of 10:52, 1 July 2008

Image:1irg.png

Template:STRUCTURE 1irg

INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9562558

About this Structure

1IRG is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family., Furui J, Uegaki K, Yamazaki T, Shirakawa M, Swindells MB, Harada H, Taniguchi T, Kyogoku Y, Structure. 1998 Apr 15;6(4):491-500. PMID:9562558

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