These data correlate well with the potential TIEG1 binding sites indentified in the Runx2 promoter as shown in Figure 5A since 10 of the 13 putative TIEG1 binding sites are contained within the −288 fragment and only 2 remain in the −92 fragment.
The smallest fragment that labeled with both anti-FLAG antibody and 8-azido-ATP was ∼15 KDa, which suggests that the binding site is contained within amino acids 411 548 of SVOP.
In this choice we are guided by the finding [9] that most of the probability for encountering a TF binding site is contained within a window of 250 base pairs (bps) located approximately 100 bps upstream of a gene.
The use of MCT1/MCT4 chimaeric transporters reveals that this binding site is contained within TM (transmembrane) helices 7 10 of MCT1.
Our results suggest that an ssDNA binding site is contained within the OB-fold (978−1078) domain (we were unable to purify the isolated OB-domain).
Analysis of the locations of the HSF binding sites revealed that 57% were contained within genes with approximately 2/3rds of these sites being in introns.
A third observation is that the identified forkhead element is immediately flanked by a potential binding site for members of the doublesex and mab-3 related transcription factor (DMRT) family so that the core sequence of this binding site (A/T,TGT) [53] is contained within the highly conserved 14bp region (Fig. 6).
The use of MCT1/MCT4 chimaeric transporters reveals that the binding site for AR-C155858 is contained within the C-terminal half of the transporter.
Measurement of the inhibitor sensitivity of several chimaeric transporters combining different domains of MCT1 and MCT4 revealed that the binding site for AR-C155858 is contained within the C-terminal half of MCT1, and involves TM (transmembrane) domains 7 10.
We have demonstrated that a binding site for factor Xa is contained within the heavy chain of the cofactor (15, 16), and we have recently shown that two residues from the central portion of the heavy chain of factor Va (amino acid residues 334 and 335) are crucial for cofactor function (17).
We have demonstrated that a binding site for factor Xa is contained within the heavy chain of the cofactor (16, 17), and we have established that the COOH terminus of the factor Va heavy chain (amino acids 680−709) is essential for optimal expression of cofactor activity because it promotes a productive interaction with prothrombin, regulating the rate of cleavage at Arg by prothrombinase (18− 218−
