2gzk
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2gzk.gif|left|200px]] | + | [[Image:2gzk.gif|left|200px]] |
| - | + | ||
| - | '''Structure of a complex of tandem HMG boxes and DNA''' | + | {{Structure |
| + | |PDB= 2gzk |SIZE=350|CAPTION= <scene name='initialview01'>2gzk</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of a complex of tandem HMG boxes and DNA''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2GZK is a [ | + | 2GZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens/rattus_rattus Homo sapiens/rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZK OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16813837 16813837] |
[[Category: Homo sapiens/rattus rattus]] | [[Category: Homo sapiens/rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:10:42 2008'' |
Revision as of 15:10, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 The protein is an engineered version of the AB di-domain of HMGB1, in which the A box has been replaced by the HMG box of the sequence-specific transcription factor SRY, to give SRY.B. In the SRY.B/DNA complex, both HMG boxes bind in the minor groove and contribute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
Page seeded by OCA on Thu Mar 20 17:10:42 2008
