| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-107 |
Sentence |
denotes |
Mutation analysis of the Pip interaction domain reveals critical residues for protein-protein interactions. |
| T2 |
108-295 |
Sentence |
denotes |
The PU.1 interaction partner (Pip) is a member of the interferon regulatory factor family that regulates gene expression through heterodimerization with the ETS transcription factor PU.1. |
| T3 |
296-445 |
Sentence |
denotes |
Binding of Pip alone to DNA is weak, and usually it is recruited by phosphorylated PU.1 to form a strong ternary complex with specific DNA sequences. |
| T4 |
446-694 |
Sentence |
denotes |
An approach combining sequence homology analysis, secondary structure predictions, and a precise mutational strategy has been used to determine critical residues within the Pip heterodimerization domain that contribute to ternary complex formation. |
| T5 |
695-787 |
Sentence |
denotes |
We have delimited the Pip interaction domain to residues 245-422 by using deletion analysis. |
| T6 |
788-1074 |
Sentence |
denotes |
Site-directed mutagenesis of conserved polar amino acids within two predicted alpha-helices contained in this region, and which are highly conserved in the IRF family, confirmed the importance of these residues for Pip-PU.1 interaction with DNA as well as for trans-activation activity. |
| T7 |
1075-1284 |
Sentence |
denotes |
Our results suggest the existence of a functional epitope essential for heterodimerization between Pip and PU.1 and possibly, in general, between interferon regulatory factor family members and their partners. |
