Structural proteomics based investigation of DNA binding domain (DBD) of FOXO4 transcription factor in complex with DNA binding element (DNA)
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ABSTRACT: The limited information available on the structure of complexes involving transcription factors and cognate DNA response elements represents a major obstacle in the quest to understand their mechanism of action at the molecular level. We implemented a concerted structural proteomics approach, which combined hydrogen-deuterium exchange (HDX), quantitative protein-protein and protein-nucleic acid cross-linking (XL), and homology analysis, to model the structure of the complex between the full-length DNA binding domain (DBD) of FOXO4 and its DNA binding element (DBE).
INSTRUMENT(S):
ORGANISM(S): Homo Sapiens (human) Escherichia Coli
SUBMITTER:
Lukáš Slavata
LAB HEAD: Petr Novak
PROVIDER: PXD013969 | Pride | 2020-05-26
REPOSITORIES: Pride
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