1w4s
From Proteopedia
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Revision as of 13:32, 5 November 2007
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CRYSTAL STRUCTURE OF THE PROXIMAL BAH DOMAIN OF POLYBROMO
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 with CL as ligand. Structure known Active Site: AC1. 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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