scholarly journals Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis

Nature ◽  
2011 ◽  
Vol 473 (7348) ◽  
pp. 536-539 ◽  
Author(s):  
Adelaine K. W. Leung ◽  
Kiyoshi Nagai ◽  
Jade Li
Keyword(s):  
Core Domain ◽  
Snrnp Core

Use of RNA Tertiary Interaction Modules for the Crystallisation of the Spliceosomal snRNP Core Domain

2010 ◽  
Vol 402 (1) ◽  
pp. 154-164 ◽  
Author(s):  
Adelaine K.W. Leung ◽  
Christian Kambach ◽  
Yasushi Kondo ◽  
Martin Kampmann ◽  
Martin Jinek ◽  
...  
Keyword(s):  
Core Domain ◽  
Tertiary Interaction ◽  
Snrnp Core

scholarly journals Re-refinement of the spliceosomal U4 snRNP core-domain structure

2016 ◽  
Vol 72 (1) ◽  
pp. 131-146 ◽  
Author(s):  
Jade Li ◽  
Adelaine K. Leung ◽  
Yasushi Kondo ◽  
Chris Oubridge ◽  
Kiyoshi Nagai
Keyword(s):  
Domain Structure ◽  
Early Model ◽  
Molecular Replacement ◽  
Model Errors ◽  
Sm Proteins ◽  
Core Domain ◽  
Small Nuclear Ribonucleoprotein ◽  
Experimental Phasing ◽  
Using Data ◽  
Snrnp Core

The core domain of small nuclear ribonucleoprotein (snRNP), comprised of a ring of seven paralogous proteins bound around a single-stranded RNA sequence, functions as the assembly nucleus in the maturation of U1, U2, U4 and U5 spliceosomal snRNPs. The structure of the human U4 snRNP core domain was initially solved at 3.6 Å resolution by experimental phasing using data with tetartohedral twinning. Molecular replacement from this model followed by density modification using untwinned data recently led to a structure of the minimal U1 snRNP at 3.3 Å resolution. With the latter structure providing a search model for molecular replacement, the U4 core-domain structure has now been re-refined. The U4 Sm site-sequence AAUUUUU has been shown to bind to the seven Sm proteins SmF–SmE–SmG–SmD3–SmB–SmD1–SmD2in an identical manner as the U1 Sm-site sequence AAUUUGU, except in SmD1where the bound U replaces G. The progression from the initial to the re-refined structure exemplifies a tortuous route to accuracy: where well diffracting crystals of complex assemblies are initially unavailable, the early model errors are rectified by exploiting preliminary interpretations in further experiments involving homologous structures. New insights are obtained from the more accurate model.

scholarly journals Targeting neddylation E2s: a novel therapeutic strategy in cancer

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Yi-Chao Zheng ◽  
Yan-Jia Guo ◽  
Bo Wang ◽  
Chong Wang ◽  
M. A. A. Mamun ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Therapeutic Strategy ◽  
Neural Precursor Cell ◽  
Catalytic Core Domain ◽  
Catalytic Core ◽  
Core Domain ◽  
E3 Ligases ◽  
Ubiquitin Conjugating Enzyme ◽  
E2 Enzymes ◽  
Conjugating Enzyme

AbstractUbiquitin-conjugating enzyme E2 M (UBE2M) and ubiquitin-conjugating enzyme E2 F (UBE2F) are the two NEDD8-conjugating enzymes of the neddylation pathway that take part in posttranslational modification and change the activity of target proteins. The activity of E2 enzymes requires both a 26-residue N-terminal docking peptide and a conserved E2 catalytic core domain, which is the basis for the transfer of neural precursor cell-expressed developmentally downregulated 8 (NEDD8). By recruiting E3 ligases and targeting cullin and non-cullin substrates, UBE2M and UBE2F play diverse biological roles. Currently, there are several inhibitors that target the UBE2M-defective in cullin neddylation protein 1 (DCN1) interaction to treat cancer. As described above, this review provides insights into the mechanism of UBE2M and UBE2F and emphasizes these two E2 enzymes as appealing therapeutic targets for the treatment of cancers.

scholarly journals Immunotherapy using algal-produced Ara h 1 core domain suppresses peanut allergy in mice

2016 ◽  
Vol 14 (7) ◽  
pp. 1541-1550 ◽  
Author(s):  
James A. Gregory ◽  
Ariel Shepley-McTaggart ◽  
Michelle Umpierrez ◽  
Barry K. Hurlburt ◽  
Soheila J. Maleki ◽  
...  
Keyword(s):  
Peanut Allergy ◽  
Core Domain ◽  
Ara H 1

scholarly journals Intravirion Generation of the C-Terminal Core Domain of HIV-1 Nef by the HIV-1 Protease Is Insufficient to Enhance Viral Infectivity

Virology ◽  
1997 ◽  
Vol 234 (2) ◽  
pp. 215-225 ◽  
Author(s):  
Michael D. Miller ◽  
Maria T. Warmerdam ◽  
Sharon S. Ferrell ◽  
Robert Benitez ◽  
Warner C. Greene
Keyword(s):  
Viral Infectivity ◽  
Core Domain ◽  
Hiv 1
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