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1W4S

Crystal structure of the proximal BAH domain of polybromo

Summary for 1W4S
Entry DOI10.2210/pdb1w4s/pdb
DescriptorPOLYBROMO 1 PROTEIN, CHLORIDE ION (3 entities in total)
Functional Keywordspolybromo, bah, bromo-associated homology domain, chromatin remodelling, pbaf, swi/snf-b, rsc, nuclear protein
Biological sourceGALLUS GALLUS (CHICKEN)
Cellular locationNucleus: Q90941
Total number of polymer chains1
Total formula weight20361.81
Authors
Oliver, A.W.,Roe, S.M.,Pearl, L.H. (deposition date: 2004-07-28, release date: 2005-04-27, Last modification date: 2024-05-08)
Primary citationOliver, A.W.,Jones, S.A.,Roe, S.M.,Matthews, S.,Goodwin, G.H.,Pearl, L.H.
Crystal Structure of the Proximal Bah Domain of the Polybromo Protein
Biochem.J., 389:657-, 2005
Cited by
PubMed 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.
PubMed: 15839835
DOI: 10.1042/BJ20050310
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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