2irf
From Proteopedia
(New page: 200px<br /><applet load="2irf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2irf, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2irf.gif|left|200px]]<br /><applet load="2irf" size=" | + | [[Image:2irf.gif|left|200px]]<br /><applet load="2irf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2irf, resolution 2.2Å" /> | caption="2irf, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF AN IRF-2/DNA COMPLEX.'''<br /> | '''CRYSTAL STRUCTURE OF AN IRF-2/DNA COMPLEX.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | There has been growing interest in the role of the IRF (interferon | + | There has been growing interest in the role of the IRF (interferon regulatory factor) family of transcription factors in the regulation of immune responses, cytokine signaling, and oncogenesis. These members are characterized by their well-conserved DNA binding domains at the N-terminal regions. Here we report the 2.2 A resolution crystal structure of the DNA binding domain of one such family member, IRF-2, bound to DNA. The structure reveals its recognition sequence, AANNGAAA (here, recognized bases are underlined and in bold, and N indicates any base), and its cooperative binding to a tandem repeat of the GAAA core sequence induced by DNA structure distortions. These facts explain well the diverse binding properties of the IRF family members, which bind to both single and tandemly repeated sequences. Furthermore, we also identified the 'helix-hairpin-strand motif' at the C terminus of the recognition helix as a metal binding site that is commonly found in certain classes of DNA-interactive proteins. Our results provide new insights into the structure and function of this family of transcription factors. |
==About this Structure== | ==About this Structure== | ||
| - | 2IRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2IRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IRF OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:10 2008'' |
Revision as of 15:55, 21 February 2008
|
CRYSTAL STRUCTURE OF AN IRF-2/DNA COMPLEX.
Overview
There has been growing interest in the role of the IRF (interferon regulatory factor) family of transcription factors in the regulation of immune responses, cytokine signaling, and oncogenesis. These members are characterized by their well-conserved DNA binding domains at the N-terminal regions. Here we report the 2.2 A resolution crystal structure of the DNA binding domain of one such family member, IRF-2, bound to DNA. The structure reveals its recognition sequence, AANNGAAA (here, recognized bases are underlined and in bold, and N indicates any base), and its cooperative binding to a tandem repeat of the GAAA core sequence induced by DNA structure distortions. These facts explain well the diverse binding properties of the IRF family members, which bind to both single and tandemly repeated sequences. Furthermore, we also identified the 'helix-hairpin-strand motif' at the C terminus of the recognition helix as a metal binding site that is commonly found in certain classes of DNA-interactive proteins. Our results provide new insights into the structure and function of this family of transcription factors.
About this Structure
2IRF is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences., Fujii Y, Shimizu T, Kusumoto M, Kyogoku Y, Taniguchi T, Hakoshima T, EMBO J. 1999 Sep 15;18(18):5028-41. PMID:10487755
Page seeded by OCA on Thu Feb 21 17:55:10 2008
