Published April 1, 2019
| Version v1
Journal article
Sequential backbone resonance assignment of AT-rich interaction domain of human BAF200
- 1. Indian Institute of Science, Molecular Biophysics Unit (India)
Description
BAF200 is a subunit of PBAF chromatin remodeling complex that contains an N-terminal AT-rich interaction domain (ARID). ARID domain in general has been shown to bind to the AT-rich DNA sequences. The human BAF200 ARID (~ 110 residues) has the potential to bind the DNA sequences with high affinity, however, the structure and the exact contribution of hBAF200 ARID in PBAF functions as well its DNA binding specificities have not been established. In this study, we have expressed and purified the hBAF200 ARID for NMR studies. We report the complete backbone 1H, 13C, and 15N chemical shift assignment and secondary structure of hBAF200 ARID domain.
Additional details
Identifiers
Publishing Information
- Journal Title
- Biomolecular NMR Assignments (Online)
- Journal Volume
- 13
- Journal Issue
- 1
- Journal Page Range
- p. 115-119
- ISSN
- 1874-270X
INIS
- Country of Publication
- Netherlands
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 54063651
- Subject category
- S62: RADIOLOGY AND NUCLEAR MEDICINE; S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- AFFINITY; CARBON 13; CHEMICAL SHIFT; CHROMATIN; DNA; HYDROGEN 1; NITROGEN 15; NUCLEAR MAGNETIC RESONANCE; RESIDUES; SPECIFICITY
- Descriptors DEC
- CARBON ISOTOPES; EVEN-ODD NUCLEI; HYDROGEN ISOTOPES; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; NITROGEN ISOTOPES; NUCLEI; NUCLEIC ACIDS; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; RESONANCE; STABLE ISOTOPES
Optional Information
- Copyright
- Copyright (c) 2019 Springer Nature B.V.