1w4s | pdb_00001w4s

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CRYSTAL STRUCTURE OF THE PROXIMAL BAH DOMAIN OF POLYBROMO

File:1w4s.gif


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1w4s, resolution 1.55Å
Sites: AC1
Ligands: CL
Coordinates: save as pdb, mmCIF, xml



Overview

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.

About this Structure

1W4S is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the proximal BAH domain of the polybromo protein., Oliver AW, Jones SA, Roe SM, Matthews S, Goodwin GH, Pearl LH, Biochem J. 2005 Aug 1;389(Pt 3):657-64. PMID:15839835

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