Transcription Factor
Accessions: | 1le9_B (3D-footprint 20231221), 1le9_F (3D-footprint 20231221), 1lei_B (3D-footprint 20231221), 1nfk_A (3D-footprint 20231221), 1nfk_B (3D-footprint 20231221), 1vkx_B (3D-footprint 20231221), 2i9t_B (3D-footprint 20231221), 3gut_B (3D-footprint 20231221), 3gut_D (3D-footprint 20231221), 3gut_F (3D-footprint 20231221), 3gut_H (3D-footprint 20231221) |
Names: | DNA-binding factor KBF1, EBP-1, NF-kappa-B1 p84/NF-kappa-B1 p98, NFKB1_MOUSE, Nuclear factor NF-kappa-B p105 subunit, NUCLEAR FACTOR NF-KAPPA-B P50 SUBUNIT, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1, NUCLEAR FACTOR KAPPA-B (NF-KB), NF-KAPPA B P50 SUBUNIT, NFKB1_HUMAN |
Organisms: | Mus musculus, Homo sapiens |
Libraries: | 3D-footprint 20231221 1 1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed] |
Uniprot: | P25799 |
Length: | 312 |
Pfam Domains: | 4-202 Rel homology domain (RHD) |
Sequence: (in bold interface residues) | 1 GPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLV 60 61 TNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEA 120 121 CIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAFL 180 181 PDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDI 240 241 QIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLE 300 301 TSEPKPFLYYPE |
Interface Residues: | 16, 18, 19, 21, 22, 24, 25, 26, 203, 205, 234, 267, 294, 295 |
3D-footprint Homologues: | 1a3q_A, 2o61_A, 1gji_A, 2ram_A, 1nfk_A, 7cli_B, 1p7h_L |
Binding Motifs: | 1le9_AB aGGAaaGTCC 1le9_EF GGAAGTC 1lei_AB TGGGnnngTACA 1nfk_A kCCC 1nfk_AB GGGAatTCCC 1vkx_AB GGAanGTCCCa 1vkx_B GGGAC 2i9t_AB GGaanTtCCC 2i9t_B ttCCC 3gut_ABD GTCCCnnnnGGAAnGTCC 3gut_CF GTCCAnTGGAA 3gut_EGH TTCCgnnnGGGACnTTCCa |
Binding Sites: | 1vkx_C 1le9_C 1le9_D 1le9_G 1le9_H 1lei_C 1nfk_C / 1nfk_D 1vkx_D 2i9t_C 2i9t_D 3gut_I / 3gut_X 3gut_J / 3gut_Y 1lei_D |
Publications: | Berkowitz B, Huang D.B, Chen-Park F.E, Sigler P.B, Ghosh G. The x-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to the interferon beta -kappa B site. The Journal of biological chemistry 277:24694-700 (2002). [Pubmed] Chen-Park F.E, Huang D.B, Noro B, Thanos D, Ghosh G. The kappa B DNA sequence from the HIV long terminal repeat functions as an allosteric regulator of HIV transcription. The Journal of biological chemistry 277:24701-8 (2002). [Pubmed] Ghosh G., van Duyne G., Ghosh S., Sigler P. B. Structure of NF-kappaB p50 homodimer bound to a kappaB site. Nature 373:303-310 (1995). [Pubmed] Chen F.E, Huang D.B, Chen Y.Q, Ghosh G. Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA. Nature 391:410-3 (1998). [Pubmed] Escalante C.R, Shen L, Thanos D, Aggarwal A.K. Structure of NF-kappaB p50/p65 heterodimer bound to the PRDII DNA element from the interferon-beta promoter. Structure (London, England : 1993) 10:383-91 (2002). [Pubmed] Stroud J.C, Oltman A, Han A, Bates D.L, Chen L. Structural basis of HIV-1 activation by NF-kappaB--a higher-order complex of p50:RelA bound to the HIV-1 LTR. Journal of molecular biology 393:98-112 (2009). [Pubmed] |
Related annotations: | PaperBLAST |
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These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.