Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A

Nature ◽  
1990 ◽  
Vol 348 (6301) ◽  
pp. 515-520 ◽  
Author(s):  
Kiyoshi Nagai ◽  
Chris Oubridge ◽  
Timm H. Jessen ◽  
Jade Li ◽  
Philip R. Evans
Keyword(s):  
Crystal Structure ◽  
Rna Binding ◽  
Binding Domain ◽  
Small Nuclear Ribonucleoprotein ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

scholarly journals T Cell Immunity in Connective Tissue Disease Patients Targets the RNA Binding Domain of the U1-70kDa Small Nuclear Ribonucleoprotein

2002 ◽  
Vol 169 (6) ◽  
pp. 3429-3437 ◽  
Author(s):  
Eric L. Greidinger ◽  
Mark F. Foecking ◽  
Kim R. Schäfermeyer ◽  
Craig W. Bailey ◽  
Shannon L. Primm ◽  
...  
Keyword(s):  
T Cell ◽  
Connective Tissue ◽  
Connective Tissue Disease ◽  
Rna Binding ◽  
Binding Domain ◽  
T Cell Immunity ◽  
Small Nuclear Ribonucleoprotein ◽  
Cell Immunity ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein

1997 ◽  
Vol 4 (11) ◽  
pp. 896-899 ◽  
Author(s):  
Jinsong Liu ◽  
Patricia A. Lynch ◽  
Chen-ya Chien ◽  
Gaetano T. Montelione ◽  
Robert M. Krug ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Influenza Virus ◽  
Rna Binding ◽  
Binding Domain ◽  
Ns1 Protein ◽  
Rna Binding Domain

scholarly journals The U1 small nuclear ribonucleoprotein (snRNP) 70K protein is transported independently of U1 snRNP particles via a nuclear localization signal in the RNA-binding domain.

1994 ◽  
Vol 14 (7) ◽  
pp. 4662-4670 ◽  
Author(s):  
J M Romac ◽  
D H Graff ◽  
J D Keene
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Rna Binding ◽  
Binding Domain ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Small Nuclear Ribonucleoprotein ◽  
Localization Signal ◽  
Nuclear Ribonucleoprotein

Expression of the recombinant human U1-70K protein in COS cells resulted in its rapid transport to the nucleus, even when binding to U1 RNA was debilitated. Deletion analysis of the U1-70K protein revealed the existence of two segments of the protein which were independently capable of nuclear localization. One nuclear localization signal (NLS) was mapped within the U1 RNA-binding domain and consists of two typically separated but interdependent elements. The major element of this NLS resides in structural loop 5 between the beta 4 strand and the alpha 2 helix of the folded RNA recognition motif. The C-terminal half of the U1-70K protein which was capable of nuclear entry contains two arginine-rich regions, which suggests the existence of a second NLS. Site-directed mutagenesis of the RNA recognition motif NLS demonstrated that the U1-70K protein can be transported independently of U1 RNA and that its association with the U1 small nuclear ribonucleoprotein particle can occur in the nucleus.

scholarly journals A specific 31-nucleotide domain of U1 RNA directly interacts with the 70K small nuclear ribonucleoprotein component.

1989 ◽  
Vol 9 (11) ◽  
pp. 4872-4881 ◽  
Author(s):  
C C Query ◽  
R C Bentley ◽  
J D Keene
Keyword(s):  
Nucleotide Sequence ◽  
Splice Site ◽  
Rna Binding ◽  
Binding Domain ◽  
Specific Domain ◽  
Stem Loop ◽  
Small Nuclear Ribonucleoprotein ◽  
Associated Proteins ◽  
Nuclear Ribonucleoprotein

We have defined the nucleotide sequence of a protein-binding domain within U1 RNA that specifically recognizes and binds both to a U1 small nuclear ribonucleoprotein component (the 70K protein) and to the previously defined RNA-binding domain of the 70K protein. We have investigated direct interactions between purified U1 RNA and 70K protein by reconstitution in vitro. Thirty-one nucleotides of U1 RNA, corresponding to stem-loop I, were required for this interaction. Nucleotides at the 5' end of U1 RNA that are involved in base pairing with the 5' splice site of pre-mRNA were not required for binding. In contrast to other reports, these findings demonstrate that a specific domain of U1 RNA can bind directly to the 70K protein independently of any other snRNP-associated proteins.

scholarly journals Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

2020 ◽  
Author(s):  
Sisi Kang ◽  
Mei Yang ◽  
Zhongsi Hong ◽  
Liping Zhang ◽  
Zhaoxia Huang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nucleocapsid Protein ◽  
Rna Binding ◽  
Structural Information ◽  
Antiviral Drug ◽  
Binding Domain ◽  
Binding Studies ◽  
Terminal Domain ◽  
Rna Binding Domain

AbstractThe outbreak of coronavirus disease (COVID-19) in China caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. It is currently no specific viral protein targeted therapeutics yet. Viral nucleocapsid protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein is yet to be clear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although overall structure is similar with other reported coronavirus nucleocapsid protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the β-sheet core. Complemented by in vitro binding studies, our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2.

Sign in / Sign up

Export Citation Format

Share Document