نتایج جستجو برای: major groove

تعداد نتایج: 626708  

Journal: :Cell 1995
Wei Yang Thomas A Steitz

The structure of y8 resolvase complexed with a 34 bp substrate DNA has been determined at 3.0 A resolution. The DNA is sharply bent by 60 ° toward the major groove and away from the resolvase catalytic domains at the recombination crossover point. The C-terminal one third of resolvase, which was disordered in the absence of DNA, forms an arm and a 3-helix DNAbinding domain on the opposite side ...

2015
Sumbul Firdaus Mohtashim Lohani Anupam Dhasmana Mohd. Haneef

Fullerenes have attracted considerable attention due to their unique chemical structure and potential applications. In this study fullerenes (C20 to C180) were interacted with different forms of DNA i.e. A, B and Z-forms. And no such change in the binding score was observed with the change in the sequence of DNA. In fact, binding score increases with the increase in the molecular weight of the ...

2016
Ursula Schulze-Gahmen Ignacia Echeverria Goran Stjepanovic Yun Bai Huasong Lu Dina Schneidman-Duhovny Jennifer A Doudna Qiang Zhou Andrej Sali James H Hurley

HIV-1 Tat hijacks the human superelongation complex (SEC) to promote proviral transcription. Here we report the 5.9 Å structure of HIV-1 TAR in complex with HIV-1 Tat and human AFF4, CDK9, and CycT1. The TAR central loop contacts the CycT1 Tat-TAR recognition motif (TRM) and the second Tat Zn2+-binding loop. Hydrogen-deuterium exchange (HDX) shows that AFF4 helix 2 is stabilized in the TAR comp...

Journal: :Proceedings. Biological sciences 1991
I S Haworth A Rodger W G Richards

Molecular mechanics calculations of the binding of spermine to a number of solvated DNA helices have led to the development of a new model for spermine complexation. The structural details of the complexes formed with d(GCGCGCGCGC)2 and d(ATATATATAT)2 decamers allowed a rationalization of the observed experimental differences for binding to these two helices. For d(ATATATATAT)2 it was concluded...

Journal: :Science 1996
J L Battiste H Mao N S Rao R Tan D R Muhandiram L E Kay A D Frankel J R Williamson

The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparag...

Journal: :Science 1995
J D Puglisi L Chen S Blanchard A D Frankel

The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has...

2011
Chao Xu Chuanbing Bian Robert Lam Aiping Dong Jinrong Min

CFP1 is a CXXC domain-containing protein and an essential component of the SETD1 histone H3K4 methyltransferase complex. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. Here, we report crystal structures of the CFP1 CXXC domain in complex with six different CpG DNA sequences. The crescent-shaped CFP1 CXXC domain is wedged into the major groove ...

Journal: :PLoS ONE 2008
Yan Wei Mei-Hua Qu Xing-Sheng Wang Lan Chen Dong-Liang Wang Ying Liu Qian Hua Rong-Qiao He

Tau, an important microtubule associated protein, has been found to bind to DNA, and to be localized in the nuclei of both neurons and some non-neuronal cells. Here, using electrophoretic mobility shifting assay (EMSA) in the presence of DNA with different chain-lengths, we observed that tau protein favored binding to a 13 bp or a longer polynucleotide. The results from atomic force microscopy ...

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