Crystal structure of the proximal BAH domain of the polybromo protein

Roe, Mark, Goodwin, G, Jones, S, Matthews, S, Pearl, L and Roe, S (2005) Crystal structure of the proximal BAH domain of the polybromo protein. Biochemistry, 389 (3). pp. 657-664.

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Abstract

The BAH domain (bromo-associated homology domain) was first identified from a repeated motif found in the nuclear protein polybromo--a large (187 kDa) modular protein comprising six bromodomains, two BAH domains and an HMG box. To date, the BAH domain has no ascribed function, although it is found in a wide range of proteins that contain additional domains involved in either transcriptional regulation (e.g. SET, PHD and bromodomain) and/or DNA binding (HMG box and AT hook). The molecular function of polybromo itself also remains unclear, but it has been identified as a key component of an SWI/SNF (switching/sucrose non-fermenting)-related, ATP-dependent chromatin-remodelling complex PBAF (polybromo, BRG1-associated factors; also known as SWI/SNF-B or SWI/SNFbeta). We present in this paper the crystal structure of the proximal BAH domain from chicken polybromo (BAH1), at a resolution of 1.6 A (1 A=0.1 nm). Structure-based sequence analysis reveals several features that may be involved in mediating protein-protein interactions.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Mark Roe
Date Deposited: 06 Feb 2012 19:15
Last Modified: 16 Jul 2012 11:33
URI: http://sro.sussex.ac.uk/id/eprint/19753
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