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Hsf1 contains DNA binding and trimerization domains and is hyper-phosphorylated in serine and threonine residues in response to heat and oxidative stress [ 39, 76], modifications that activate its transcriptional activity [ 39, 76].
Given that the highest degree of sequence similarity between hHSF1, hHSF2, and dHSF is in the DNA binding and trimerization domains (DBD-TD) and that the previously selected dHSF aptamer was found to bind the DBD-TD of dHSF, we predict these novel hHSF aptamers are likely to bind the HSF proteins in a similar fashion.
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Here we review the current knowledge of the structure and function of these trimerization domains.
The positions and orientations of the transport domains relative to the trimerization domains remain essentially unchanged in the apo and fully bound forms of GltPh-R397A and GltPhin.
We wanted to point out that the positions and orientations of the transport domains relative to the trimerization domains are the same in the apo and fully bound forms.
Although both mFasL and sFasL contain the trimerization domain and can bind the Fas receptor, the naturally cleaved form of sFasL is unable to oligomerize the Fas receptor and trigger apoptosis.
Trimerization domains are non-collagenous domains of very different structures.
For the proper folding of the triple helix collagens contain trimerization domains.
The size of trimerization domains varies from 35 residues in type IX collagen to around 250 residues for the fibrillar collagens.
The helical neck domains form independent trimerization domains.
Are the authors only comparing the trimerization domains?
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