Crystal structure of the proximal BAH domain of the polybromo protein.
MetadataShow full item record
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.
Version of record
Amino Acid Sequence
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Molecular Sequence Data
License start date
The Biochemical journal, 2005, 389 (Pt 3), pp. 657 - 664
Showing items related by title, author, creator and subject.
PHOX2B analysis in non-syndromic neuroblastoma cases shows novel mutations and genotype-phenotype associations. McConville, C; Reid, S; Baskcomb, L; Douglas, J; Rahman, N (2006-06)Neuroblastoma (NB) is an embryonal tumor originating from neural crest cells and is one of the most common solid tumors of childhood. Recently, constitutional mutations in PHOX2B have been shown to confer an increased risk ...
Gould, CM; Diella, F; Via, A; Puntervoll, P; Gemünd, C; Chabanis-Davidson, S; Michael, S; Sayadi, A; Bryne, JC; Chica, C; Seiler, M; Davey, NE; Haslam, N; Weatheritt, RJ; Budd, A; Hughes, T; Pas, J; Rychlewski, L; Travé, G; Aasland, R; Helmer-Citterich, M; Linding, R; Gibson, TJ (2010-01)Linear motifs are short segments of multidomain proteins that provide regulatory functions independently of protein tertiary structure. Much of intracellular signalling passes through protein modifications at linear motifs. ...
Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment. Xiong, S; Lorenzen, K; Couzens, AL; Templeton, CM; Rajendran, D; Mao, DYL; Juang, Y-C; Chiovitti, D; Kurinov, I; Guettler, S; Gingras, A-C; Sicheri, F (2018-08)The human NDR family kinases control diverse aspects of cell growth, and are regulated through phosphorylation and association with scaffolds such as MOB1. Here, we report the crystal structure of the human NDR1 kinase ...