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Structural proteomics based investigation of DNA binding domain (DBD) of FOXO4 transcription factor in complex with DNA binding element (DNA)

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): solariX

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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MS-Based Approaches Enable the Structural Characterization of Transcription Factor/DNA Response Element Complex.

Slavata Lukáš L Chmelík Josef J Kavan Daniel D Filandrová Růžena R Fiala Jan J Rosůlek Michal M Mrázek Hynek H Kukačka Zdeněk Z Vališ Karel K Man Petr P Miller Michael M McIntyre William W Fabris Daniele D Novák Petr P

Biomolecules 20190926 10

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-leng ...[more]

PMID: 31561554

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