Abstract
In this study, we describe a new approach for studying protein-DNA interactions in solution. The approach is based on mapping the UV laser-induced protein-DNA cross-links between the amino acids of the protein and the DNA bases that are in direct contact. The approach was applied for studying the solution structure of the human necrosis factor (NF)-κB p50 homodimer bound to a 37 base pair DNA. Several points of contact identical to those observed in the NF-κB-DNA crystal structure were found between the two biomolecules. Evidence is provided for the occurrence of two new contact points, one for each DNA strand. These new points of contact are located symmetrically a base apart from the extremity of the binding sequence.
| Original language | English |
|---|---|
| Pages (from-to) | 592-596 |
| Number of pages | 5 |
| Journal | Photochemistry and Photobiology |
| Volume | 77 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jun 2003 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
Cite this
Solution Study of the NF-κB p50-DNA Complex by UV Laser Protein-DNA Cross-linking. / Angelov, Dimitar; Charra, Monique; Müller, Christoph W.; Cadet, Jean; Dimitrov, Stefan.
In: Photochemistry and Photobiology, Vol. 77, No. 6, 06.2003, p. 592-596.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solution Study of the NF-κB p50-DNA Complex by UV Laser Protein-DNA Cross-linking
AU - Angelov, Dimitar
AU - Charra, Monique
AU - Müller, Christoph W.
AU - Cadet, Jean
AU - Dimitrov, Stefan
PY - 2003/6
Y1 - 2003/6
N2 - In this study, we describe a new approach for studying protein-DNA interactions in solution. The approach is based on mapping the UV laser-induced protein-DNA cross-links between the amino acids of the protein and the DNA bases that are in direct contact. The approach was applied for studying the solution structure of the human necrosis factor (NF)-κB p50 homodimer bound to a 37 base pair DNA. Several points of contact identical to those observed in the NF-κB-DNA crystal structure were found between the two biomolecules. Evidence is provided for the occurrence of two new contact points, one for each DNA strand. These new points of contact are located symmetrically a base apart from the extremity of the binding sequence.
AB - In this study, we describe a new approach for studying protein-DNA interactions in solution. The approach is based on mapping the UV laser-induced protein-DNA cross-links between the amino acids of the protein and the DNA bases that are in direct contact. The approach was applied for studying the solution structure of the human necrosis factor (NF)-κB p50 homodimer bound to a 37 base pair DNA. Several points of contact identical to those observed in the NF-κB-DNA crystal structure were found between the two biomolecules. Evidence is provided for the occurrence of two new contact points, one for each DNA strand. These new points of contact are located symmetrically a base apart from the extremity of the binding sequence.
UR - http://www.scopus.com/inward/record.url?scp=0344034180&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0344034180&partnerID=8YFLogxK
U2 - 10.1562/0031-8655(2003)077<0592:SSOTNP>2.0.CO;2
DO - 10.1562/0031-8655(2003)077<0592:SSOTNP>2.0.CO;2
M3 - Article
C2 - 12870843
AN - SCOPUS:0344034180
VL - 77
SP - 592
EP - 596
JO - Photochemistry and Photobiology
JF - Photochemistry and Photobiology
SN - 0031-8655
IS - 6
ER -