| Range |
~0.4 kcal/mol
|
| Organism |
Unspecified |
| Reference |
Serber Z, Ferrell JE Jr. Tuning bulk electrostatics to regulate protein function. Cell. 2007 Feb 9 128(3):441-4. p.442 right column bottom paragraphPubMed ID17289565
|
| Primary Source |
Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science. 2005 Jul 1 309(5731):142-5. fig 1EPubMed ID15994560
|
| Method |
(Primary source) "To gauge the effect of differential phosphorylation on activity, [researchers] mimicked in vivo phosphorylation by mutating phospho acceptor serines to alanines singly and in pairs (Fig. 1C), and [they] then measured the DNA binding affinity of phosphorylated and unmodified forms." In vitro |
| Comments |
"There are also parallels between Ste5 and Ets1, a transcription factor whose DNA binding is regulated by three clustered CaMKII phosphorylation sites. Each phosphorylation in Ets1 successively decreases the affinity of Ets1 for DNA, by about 0.4 kcal/mol (primary source), less than that measured by McLaughlin and assumed here for Ste5." See fig. 1E in primary source |
| Entered by |
Uri M |
| ID |
105725 |