1zk9
From Proteopedia
(New page: 200px<br /><applet load="1zk9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zk9, resolution 2.18Å" /> '''NF-kB RelB forms an ...) |
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| - | [[Image:1zk9.gif|left|200px]]<br /><applet load="1zk9" size=" | + | [[Image:1zk9.gif|left|200px]]<br /><applet load="1zk9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zk9, resolution 2.18Å" /> | caption="1zk9, resolution 2.18Å" /> | ||
'''NF-kB RelB forms an intertwined homodimer'''<br /> | '''NF-kB RelB forms an intertwined homodimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray structure of the RelB dimerization domain (DD) reveals that the | + | The X-ray structure of the RelB dimerization domain (DD) reveals that the RelBDD assumes an unexpected intertwined fold topology atypical of other NF-kappaB dimers. All typical NF-kappaB dimers are formed by the association of two independently folded immunoglobulin (Ig) domains. In RelBDD, two polypeptides reconstruct both Ig domains in the dimer with an extra beta sheet connecting the two domains. Residues most critical to NF-kappaB dimer formation are invariant in RelB, and Y300 plays a positive role in RelBDD dimer formation. The presence of RelB-specific nonpolar residues at the surface removes several intradomain surface hydrogen bonds that may render the domain fold unstable. Intertwining may stabilize the RelBDD homodimer by forming the extra beta sheet. We show that, as in the crystal, RelB forms an intertwined homodimer in solution. We suggest that the transiently stable RelB homodimer might prevent its rapid degradation, allowing for heterodimer formation with p50 and p52. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1ZK9 is a [http://en.wikipedia.org/wiki/Single_protein 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=1ZK9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ghosh, G.]] | [[Category: Ghosh, G.]] | ||
| - | [[Category: Huang, D | + | [[Category: Huang, D B.]] |
[[Category: Vu, D.]] | [[Category: Vu, D.]] | ||
[[Category: intertwined dimer]] | [[Category: intertwined dimer]] | ||
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[[Category: transcription factors]] | [[Category: transcription factors]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:30 2008'' |
Revision as of 14:16, 21 February 2008
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NF-kB RelB forms an intertwined homodimer
Overview
The X-ray structure of the RelB dimerization domain (DD) reveals that the RelBDD assumes an unexpected intertwined fold topology atypical of other NF-kappaB dimers. All typical NF-kappaB dimers are formed by the association of two independently folded immunoglobulin (Ig) domains. In RelBDD, two polypeptides reconstruct both Ig domains in the dimer with an extra beta sheet connecting the two domains. Residues most critical to NF-kappaB dimer formation are invariant in RelB, and Y300 plays a positive role in RelBDD dimer formation. The presence of RelB-specific nonpolar residues at the surface removes several intradomain surface hydrogen bonds that may render the domain fold unstable. Intertwining may stabilize the RelBDD homodimer by forming the extra beta sheet. We show that, as in the crystal, RelB forms an intertwined homodimer in solution. We suggest that the transiently stable RelB homodimer might prevent its rapid degradation, allowing for heterodimer formation with p50 and p52.
About this Structure
1ZK9 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
NF-kappaB RelB forms an intertwined homodimer., Huang DB, Vu D, Ghosh G, Structure. 2005 Sep;13(9):1365-73. PMID:16154093
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