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2BZ2

Solution structure of NELF E RRM

Summary for 2BZ2
Entry DOI10.2210/pdb2bz2/pdb
DescriptorNEGATIVE ELONGATION FACTOR E (1 entity in total)
Functional Keywordsnelf e, rna recognition motif, alternative splicing, nuclear protein, phosphorylation, repressor, rna-binding, transcription, transcription regulation
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationNucleus: P18615
Total number of polymer chains1
Total formula weight13384.09
Authors
Schweimer, K.,Rao, J.N.,Neumann, L.,Rosch, P.,Wohrl, B.M. (deposition date: 2005-08-10, release date: 2006-08-16, Last modification date: 2024-05-15)
Primary citationRao, J.N.,Neumann, L.,Wenzel, S.,Schweimer, K.,Rosch, P.,Wohrl, B.M.
Structural studies on the RNA-recognition motif of NELF E, a cellular negative transcription elongation factor involved in the regulation of HIV transcription.
Biochem. J., 400:449-456, 2006
Cited by
PubMed Abstract: The elongation of transcription of HIV RNA at the TAR (transactivation-response element) is highly regulated by positive and negative factors. The cellular negative transcription elongation factor NELF (negative elongation factor) was suggested to be involved in transcriptional regulation of HIV-1 (HIV type 1) by binding to the stem of the viral TAR RNA which is synthesized by cellular RNA polymerase II at the viral long terminal repeat. NELF is a heterotetrameric protein consisting of NELF A, B, C or the splice variant D, and E. In the present study, we determined the solution structure of the RRM (RNA-recognition motif) of the RNA-binding subunit NELF E and studied its interaction with the viral TAR RNA. Our results show that the separately expressed recombinant NELF E RRM has alpha-helical and beta-strand elements adopting a betaalphabetabetaalphabeta fold and is able to bind to TAR RNA. Fluorescence equilibrium titrations with fluorescently labelled double- and single-stranded oligoribonucleotides representing the TAR RNA stem imply that NELF E RRM binds to the single-stranded TAR RNAs with K(d) values in the low-micromolar range.
PubMed: 16898873
DOI: 10.1042/BJ20060421
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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