Crystal structure of the proximal BAH domain of the polybromo protein.
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.
Oliver
Antony W
AW
CR-UK DNA Repair Enzymes Group, Section of Structural Biology, The Institute of Cancer Research, 237 Fulham Road, Chelsea, London SW3 6JB, UK. antony.oliver@icr.ac.uk
Jones
Sarah A
SA
Roe
Stephen Mark
SM
Matthews
Steve
S
Goodwin
Graham H
GH
Pearl
Laurence H
LH
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D017124:Conserved Sequence; D003460:Crystallization; D004268:DNA-Binding Proteins; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry*
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C102195:PBRM1 protein, human; D014157:Transcription Factors