| dc.contributor.author |
Bukhtiyarova, M |
en |
| dc.contributor.author |
Karpusas, M |
en |
| dc.contributor.author |
Northrup, K |
en |
| dc.contributor.author |
Namboodiri, H |
en |
| dc.contributor.author |
Springman, E |
en |
| dc.date.accessioned |
2014-06-06T06:47:33Z |
|
| dc.date.available |
2014-06-06T06:47:33Z |
|
| dc.date.issued |
2007 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1021/bi0622221 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/3667 |
|
| dc.subject |
Crystal Structure |
en |
| dc.subject |
High Temperature |
en |
| dc.subject |
Map Kinase |
en |
| dc.subject |
Molecular Dynamic Simulation |
en |
| dc.subject |
Structural Dynamics |
en |
| dc.subject |
Structural Stability |
en |
| dc.subject |
Structure and Function |
en |
| dc.subject |
Structure Function |
en |
| dc.subject |
Thermal Stability |
en |
| dc.subject |
X-ray Crystal Structure |
en |
| dc.subject |
National Synchrotron Light Source |
en |
| dc.subject |
Wild Type |
en |
| dc.title |
Mutagenesis of p38alpha MAP Kinase Establishes Key Roles of Phe169 in Function and Structural Dynamics and Reveals a Novel DFG-OUT State |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1021/bi0622221 |
en |
| heal.publicationDate |
2007 |
en |
| heal.abstract |
In order to study the role of Phe169 in p38 MAP kinase structure and function, wild-type p38 and five p38 DFG motif mutants were examined in vitro for phosphorylation by MKK6, kinase activity toward ATF2 substrate, thermal stability, and X-ray crystal structure. All six p38 variants were efficiently phosphorylated by MKK6. However, only one activated p38 mutant (F169Y) possessed measurable |
en |
| heal.journalName |
Biochemistry |
en |
| dc.identifier.doi |
10.1021/bi0622221 |
en |