Pub. Date : 1993 Jan 25
PMID : 8420956
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Role of tyrosine residue 264 of RecA for the binding of cofactor and DNA. | Tyrosine | RAD51 recombinase | Homo sapiens |
2 | The tyrosine fluorescence of the RecA protein is quenched by about 15% upon binding of the cofactor analog adenosine 5"-O-(3-thiotriphosphate) (ATP gamma S). | Tyrosine | RAD51 recombinase | Homo sapiens |
3 | Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. | Tyrosine | RAD51 recombinase | Homo sapiens |
4 | Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. | Tyrosine | RAD51 recombinase | Homo sapiens |
5 | Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. | Tyrosine | RAD51 recombinase | Homo sapiens |
6 | Tyr-264 may be an important residue for the allosteric effect induced by the cofactor for the binding of DNA to RecA. | Tyrosine | RAD51 recombinase | Homo sapiens |
7 | The fact that we observe no interaction of ATP gamma S with Tyr-103 (as evidenced from absence of fluorescence change) but instead with Tyr-264 may suggest an important conformational difference between the RecA complexes with, respectively, ADP and ATP. | Tyrosine | RAD51 recombinase | Homo sapiens |