2gzk
From Proteopedia
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Structure of a complex of tandem HMG boxes and DNA
Overview
The high-mobility group protein HMGB1 contains two tandem DNA-binding HMG, box domains, A and B, linked by a short flexible linker that allows the, two domains to behave independently in the free protein. There is no, structural information on how the linked domains and linker behave when, bound to DNA, mainly due to the lack of any DNA-sequence preference of, HMGB1. We report the structure determination, by NMR spectroscopy, of a, well-defined complex of two tandem HMG boxes bound to a 16 bp, oligonucleotide. The protein is an engineered version of the AB di-domain, of HMGB1, in which the A box has been replaced by the HMG box of the, sequence-specific transcription factor SRY, to give SRY.B. In the, SRY.B/DNA complex, both HMG boxes bind in the minor groove and contribute, to the overall DNA bending by intercalation of bulky hydrophobic residues, between base-pairs; the bends reinforce each other, and the basic linker, lies partly in the minor groove. As well as being the first structure of, an HMG-box di-domain bound to DNA, this provides the first structure of, the B domain of HMGB1 bound to DNA.
About this Structure
2GZK is a Single protein structure of sequence from Homo sapiens/rattus rattus. Full crystallographic information is available from OCA.
Reference
Structure of a complex of tandem HMG boxes and DNA., Stott K, Tang GS, Lee KB, Thomas JO, J Mol Biol. 2006 Jun 30;360(1):90-104. Epub 2006 May 12. PMID:16813837
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