scholarly journals Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

2013 ◽  
Vol 181 (1) ◽  
pp. 82-88 ◽  
Author(s):  
Jennifer B. Nguyen ◽  
Yorgo Modis
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Coiled Coil ◽  
Coiled Coil Domain ◽  
Nucleic Acid Sensor

scholarly journals Crystal Structure of the YchF Protein Reveals Binding Sites for GTP and Nucleic Acid

2003 ◽  
Vol 185 (14) ◽  
pp. 4031-4037 ◽  
Author(s):  
Alexey Teplyakov ◽  
Galina Obmolova ◽  
Seung Y. Chu ◽  
John Toedt ◽  
Edward Eisenstein ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Binding Site ◽  
Coiled Coil ◽  
Genomic Analysis ◽  
Protein Fluorescence ◽  
Terminal Domain ◽  
Fluorescence Measurements ◽  
Α Helix

ABSTRACT The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 Å resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced α-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an α-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor.

scholarly journals Crystal Structure of the Central Coiled-Coil Domain from Human Liprin-β2

Biochemistry ◽  
2011 ◽  
Vol 50 (18) ◽  
pp. 3807-3815 ◽  
Author(s):  
Ryan L. Stafford ◽  
Ming-Yun Tang ◽  
Michael R. Sawaya ◽  
Martin L. Phillips ◽  
James U. Bowie
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Coiled Coil Domain

scholarly journals Crystal Structure of the Japanese Encephalitis Virus Capsid Protein

Viruses ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 623 ◽  
Author(s):  
Thanalai Poonsiri ◽  
Gareth S. A. Wright ◽  
Tom Solomon ◽  
Svetlana V. Antonyuk
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Capsid Protein ◽  
Japanese Encephalitis ◽  
Protein A ◽  
Coiled Coil ◽  
Specific Treatment ◽  
Capsid Proteins ◽  
Nucleic Acid Binding ◽  
Α Helix

Japanese encephalitis (JE) is inflammation and swelling of the brain caused by the JE virus (JEV), a mosquito-borne member of the Flavivirus family. There are around 68,000 JE cases worldwide each year, many of which result in permanent brain damage and death. There is no specific treatment for JE. Here we present the crystal structure of the JEV capsid protein, a potential drug target, at 1.98 Å, and compare it to other flavivirus capsid proteins. The JEV capsid has a helical secondary structure (α helixes 1–4) and a similar protein fold to the dengue virus (DENV), the West Nile virus (WNV), and the Zika virus (ZIKV) capsid proteins. It forms a homodimer by antiparallel pairing with another subunit (‘) through α-helix 1-1’, 2-2’, and 4-4’ interactions. This dimeric form is believed to be the building block of the nucleocapsid. The flexibility of the N-terminal α helix-1 allows the formation of closed and open conformations with possible functional importance. The basic C-terminal pairing of α4-4’ forms a coiled-coil-like structure, indicating possible nucleic acid binding functionality. However, a comparison with other nucleic acid interacting domains indicates that homodimerization would preclude binding. This is the first JEV capsid protein to be described and is an addition to the structural biology of the Flavivirus.

Crystal structure of the coiled‐coil domain of Drosophila TRIM protein Brat

2019 ◽  
Vol 87 (8) ◽  
pp. 706-710 ◽  
Author(s):  
Chunhua Liu ◽  
Zelin Shan ◽  
Jianqiao Diao ◽  
Wenyu Wen ◽  
Wenning Wang
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Trim Protein ◽  
Coiled Coil Domain

scholarly journals Crystal Structure of a Coiled-Coil Domain from Human ROCK I

PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e18080 ◽  
Author(s):  
Daqi Tu ◽  
Yiqun Li ◽  
Hyun Kyu Song ◽  
Angela V. Toms ◽  
Christopher J. Gould ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Coiled Coil Domain
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