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: 2o61_A, 1gji_A, 2ram_A, 1nfk_A, 7cli_B, 1a3q_A, 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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