scholarly journals Nuclear Magnetic Resonance Structure of an 8 × 8 Nucleotide RNA Internal Loop Flanked on Each Side by Three Watson–Crick Pairs and Comparison to Three-Dimensional Predictions

Biochemistry ◽  
2017 ◽  
Vol 56 (29) ◽  
pp. 3733-3744 ◽  
Author(s):  
Andrew D. Kauffmann ◽  
Scott D. Kennedy ◽  
Jianbo Zhao ◽  
Douglas H. Turner
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Three Dimensional ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Internal Loop ◽  
Rna Internal Loop ◽  
Nuclear Magnetic

scholarly journals Nuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain Fold

2008 ◽  
Vol 83 (4) ◽  
pp. 1823-1836 ◽  
Author(s):  
Amarnath Chatterjee ◽  
Margaret A. Johnson ◽  
Pedro Serrano ◽  
Bill Pedrini ◽  
Jeremiah S. Joseph ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Severe Acute Respiratory Syndrome ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Three Dimensional Structure ◽  
Unique Domain ◽  
Nuclear Magnetic

ABSTRACT The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for “middle of the SARS-unique domain”) in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.

Nuclear Magnetic Resonance Structure of a Prototype Lin12-Notch Repeat Module from Human Notch1†

Biochemistry ◽  
2003 ◽  
Vol 42 (23) ◽  
pp. 7061-7067 ◽  
Author(s):  
Didem Vardar ◽  
Christopher L. North ◽  
Cheryll Sanchez-Irizarry ◽  
Jon C. Aster ◽  
Stephen C. Blacklow
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nuclear Magnetic

scholarly journals Nuclear Magnetic Resonance Structure and IgE Epitopes of Blo t 5, a Major Dust Mite Allergen

2008 ◽  
Vol 181 (4) ◽  
pp. 2586-2596 ◽  
Author(s):  
Siew Leong Chan ◽  
Tan Ching Ong ◽  
Yun Feng Gao ◽  
Yuen Sung Tiong ◽  
De Yun Wang ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Mite Allergen ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Dust Mite ◽  
Dust Mite Allergen ◽  
Nuclear Magnetic
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