Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191637" target="_blank" >RIV/00216208:11310/13:10191637 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/13:00420952 RIV/00209805:_____/13:#0000414
Result on the web
<a href="http://dx.doi.org/10.1002/pmic.201300029" target="_blank" >http://dx.doi.org/10.1002/pmic.201300029</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/pmic.201300029" target="_blank" >10.1002/pmic.201300029</a>
Alternative languages
Result language
angličtina
Original language name
Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry
Original language description
MDM2 is a multidomain protein that functions as an E3 ubiquitin ligase, transcription repressor, mRNA-binding protein, translation factor, and molecular chaperone. The small molecule Nutlin-3 has been engineered to bind to the N-terminal hydrophobic pocket domain of MDM2. This binding of Nutlin-3 has two consequences: (i) antagonistic effects through competitive disruption of the MDM2-p53 complex and (ii) agonist effects that allosterically stabilize MDM2 protein-protein interactions that increase p53 ubiquitination as well as nucleophosmin deoligomerization. We present a methodology using a hydrogen/deuterium (H/D) exchange platform that measures Nutlin-3 binding to the N-terminal domain of MDM2 (MDM2(1-126)) in order to begin to develop dynamic assays that evaluate MDM2 allostery. In order to localize the regions in MDM2 being suppressed by Nutlin-3, MDM2 was incubated with the ligand and H/D amide exchange was measured after pepsin digestion. One dynamic segment containing amino aci
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proteomics
ISSN
1615-9853
e-ISSN
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Volume of the periodical
13
Issue of the periodical within the volume
16
Country of publishing house
GB - UNITED KINGDOM
Number of pages
14
Pages from-to
2512-2525
UT code for WoS article
000327008700014
EID of the result in the Scopus database
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