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Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.

Abstract：

:HMGB1 (high-mobility group B1) is a ubiquitously expressed bifunctional protein that acts as a nuclear protein in cells and also as an inflammatory mediator in the extracellular space. HMGB1 changes its functions according to the redox states in both intra- and extra-cellular environments. Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. The A-domain with the disulfide bond shows reduced affinity to cisplatin modified DNA. We have solved the oxidized A-domain structure by NMR. In the structure, Phe38 has a flipped ring orientation from that found in the reduced form; the phenyl ring in the reduced form intercalates into the platinated lesion in DNA. The phenyl ring orientation in the oxidized form is stabilized through intramolecular hydrophobic contacts. The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wang J,Tochio N,Takeuchi A,Uewaki J,Kobayashi N,Tate S

subject

Has Abstract

pub_date

2013-11-29 00:00:00

pages

701-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)01766-X

journal_volume

441

pub_type

杂志文章

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