3D1N
Structure of human Brn-5 transcription factor in complex with corticotrophin-releasing hormone gene promoter
Summary for 3D1N
Entry DOI | 10.2210/pdb3d1n/pdb |
Related | 1au7 1oct |
Descriptor | 5'-D(*DAP*DGP*DCP*DAP*DTP*DAP*DAP*DAP*DTP*DAP*DAP*DTP*DAP*DA)-3', 5'-D(*DTP*DTP*DAP*DTP*DTP*DAP*DTP*DTP*DTP*DAP*DTP*DGP*DCP*DT)-3', POU domain, class 6, transcription factor 1, ... (4 entities in total) |
Functional Keywords | protein-dna complex, helix-turn-helix (hth), dna-binding, homeobox, nucleus, transcription, transcription regulation, transcription regulator-dna complex, transcription regulator/dna |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus: 3D1N |
Total number of polymer chains | 16 |
Total formula weight | 175754.48 |
Authors | Pereira, J.H.,Ha, S.C.,Kim, S.-H. (deposition date: 2008-05-06, release date: 2009-05-26, Last modification date: 2024-10-30) |
Primary citation | Pereira, J.H.,Kim, S.H. Structure of human Brn-5 transcription factor in complex with CRH gene promoter. J.Struct.Biol., 167:159-165, 2009 Cited by PubMed Abstract: The Brn-5 protein, highly expressed in human brain, belongs to the POU family; a class of transcription factors involved in a wide variety of biological processes ranging from programming of embryonic stem cells to cellular housekeeping. This functional diversity is conferred by two DNA-binding subdomains that can assume several configurations due to a bipartite arrangement of POU-specific (POU(S)) and POU-homeo (POU(H)) subdomains separated by a linker region. The crystal structure of human Brn-5 transcription factor in complex with corticotrophin-releasing hormone (CRH) gene promoter reveals an unexpected recognition mode of the protein to its cognate DNA. Moreover, the structure also shows the role of the linker in allowing diverse configurations that can be assumed by the two subdomains. PubMed: 19450691DOI: 10.1016/j.jsb.2009.05.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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