The SARS-Unique domain (SUD) of SARS coronavirus contains two macrodomains that bind g-quadruplexes. Tan, J., Vonrhein, C., Smart, O. S, Bricogne, G., Bollati, M., Kusov, Y., Hansen, G., Mesters, J. R, Schmidt, C. L, & Hilgenfeld, R. PLoS pathogens, 5(5):e1000428 ST – The SARS–Unique Domain (SUD) of SAR, 2009. ![The SARS-Unique domain (SUD) of SARS coronavirus contains two macrodomains that bind g-quadruplexes [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex ¡title¿Author Summary¡/title¿ ¡p¿The genome of the SARS coronavirus codes for 16 non-structural proteins that are involved in replicating this huge RNA (approximately 29 kilobases). The roles of many of these in replication (and/or transcription) are unknown. We attempt to derive conclusions concerning the possible functions of these proteins from their three-dimensional structures, which we determine by X-ray crystallography. Non-structural protein 3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS-unique domain, a stretch of about 338 residues that is completely absent from any other coronavirus. It may thus be responsible for the extraordinarily high pathogenicity of the SARS coronavirus, compared to other viruses of this family. We describe here the three-dimensional structure of the SARS-unique domain and show that it consists of two modules with a known fold, the so-called macrodomain. Furthermore, we demonstrate that these domains bind unusual nucleic-acid structures formed by consecutive guanosine nucleotides, where four strands of nucleic acid are forming a superhelix (so-called G-quadruplexes). SUD may be involved in binding to viral or host-cell RNA bearing this peculiar structure and thereby regulate viral replication or fight the immune response of the infected host cell.¡/p¿
@article{Tan2009,
title = {The {SARS}-{Unique} domain ({SUD}) of {SARS} coronavirus contains two macrodomains that bind g-quadruplexes},
volume = {5},
url = {http://dx.doi.org/10.1371/journal.ppat.1000428},
doi = {10.1371/journal.ppat.1000428},
abstract = {¡title¿Author Summary¡/title¿ ¡p¿The genome of the SARS coronavirus codes for 16 non-structural proteins that are involved in replicating this huge RNA (approximately 29 kilobases). The roles of many of these in replication (and/or transcription) are unknown. We attempt to derive conclusions concerning the possible functions of these proteins from their three-dimensional structures, which we determine by X-ray crystallography. Non-structural protein 3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS-unique domain, a stretch of about 338 residues that is completely absent from any other coronavirus. It may thus be responsible for the extraordinarily high pathogenicity of the SARS coronavirus, compared to other viruses of this family. We describe here the three-dimensional structure of the SARS-unique domain and show that it consists of two modules with a known fold, the so-called macrodomain. Furthermore, we demonstrate that these domains bind unusual nucleic-acid structures formed by consecutive guanosine nucleotides, where four strands of nucleic acid are forming a superhelix (so-called G-quadruplexes). SUD may be involved in binding to viral or host-cell RNA bearing this peculiar structure and thereby regulate viral replication or fight the immune response of the infected host cell.¡/p¿},
number = {5},
journal = {PLoS pathogens},
author = {Tan, Jinzhi and Vonrhein, Clemens and Smart, Oliver S and Bricogne, Gerard and Bollati, Michela and Kusov, Yuri and Hansen, Guido and Mesters, Jeroen R and Schmidt, Christian L and Hilgenfeld, Rolf},
year = {2009},
keywords = {\#nosource},
pages = {e1000428 ST -- The SARS--Unique Domain (SUD) of SAR},
}
Downloads: 0
{"_id":"S3gko3JQSM8H8m8by","bibbaseid":"tan-vonrhein-smart-bricogne-bollati-kusov-hansen-mesters-etal-thesarsuniquedomainsudofsarscoronaviruscontainstwomacrodomainsthatbindgquadruplexes-2009","author_short":["Tan, J.","Vonrhein, C.","Smart, O. S","Bricogne, G.","Bollati, M.","Kusov, Y.","Hansen, G.","Mesters, J. R","Schmidt, C. L","Hilgenfeld, R."],"bibdata":{"bibtype":"article","type":"article","title":"The SARS-Unique domain (SUD) of SARS coronavirus contains two macrodomains that bind g-quadruplexes","volume":"5","url":"http://dx.doi.org/10.1371/journal.ppat.1000428","doi":"10.1371/journal.ppat.1000428","abstract":"¡title¿Author Summary¡/title¿ ¡p¿The genome of the SARS coronavirus codes for 16 non-structural proteins that are involved in replicating this huge RNA (approximately 29 kilobases). The roles of many of these in replication (and/or transcription) are unknown. We attempt to derive conclusions concerning the possible functions of these proteins from their three-dimensional structures, which we determine by X-ray crystallography. Non-structural protein 3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS-unique domain, a stretch of about 338 residues that is completely absent from any other coronavirus. It may thus be responsible for the extraordinarily high pathogenicity of the SARS coronavirus, compared to other viruses of this family. We describe here the three-dimensional structure of the SARS-unique domain and show that it consists of two modules with a known fold, the so-called macrodomain. Furthermore, we demonstrate that these domains bind unusual nucleic-acid structures formed by consecutive guanosine nucleotides, where four strands of nucleic acid are forming a superhelix (so-called G-quadruplexes). SUD may be involved in binding to viral or host-cell RNA bearing this peculiar structure and thereby regulate viral replication or fight the immune response of the infected host cell.¡/p¿","number":"5","journal":"PLoS pathogens","author":[{"propositions":[],"lastnames":["Tan"],"firstnames":["Jinzhi"],"suffixes":[]},{"propositions":[],"lastnames":["Vonrhein"],"firstnames":["Clemens"],"suffixes":[]},{"propositions":[],"lastnames":["Smart"],"firstnames":["Oliver","S"],"suffixes":[]},{"propositions":[],"lastnames":["Bricogne"],"firstnames":["Gerard"],"suffixes":[]},{"propositions":[],"lastnames":["Bollati"],"firstnames":["Michela"],"suffixes":[]},{"propositions":[],"lastnames":["Kusov"],"firstnames":["Yuri"],"suffixes":[]},{"propositions":[],"lastnames":["Hansen"],"firstnames":["Guido"],"suffixes":[]},{"propositions":[],"lastnames":["Mesters"],"firstnames":["Jeroen","R"],"suffixes":[]},{"propositions":[],"lastnames":["Schmidt"],"firstnames":["Christian","L"],"suffixes":[]},{"propositions":[],"lastnames":["Hilgenfeld"],"firstnames":["Rolf"],"suffixes":[]}],"year":"2009","keywords":"#nosource","pages":"e1000428 ST – The SARS–Unique Domain (SUD) of SAR","bibtex":"@article{Tan2009,\n\ttitle = {The {SARS}-{Unique} domain ({SUD}) of {SARS} coronavirus contains two macrodomains that bind g-quadruplexes},\n\tvolume = {5},\n\turl = {http://dx.doi.org/10.1371/journal.ppat.1000428},\n\tdoi = {10.1371/journal.ppat.1000428},\n\tabstract = {¡title¿Author Summary¡/title¿ ¡p¿The genome of the SARS coronavirus codes for 16 non-structural proteins that are involved in replicating this huge RNA (approximately 29 kilobases). The roles of many of these in replication (and/or transcription) are unknown. We attempt to derive conclusions concerning the possible functions of these proteins from their three-dimensional structures, which we determine by X-ray crystallography. Non-structural protein 3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS-unique domain, a stretch of about 338 residues that is completely absent from any other coronavirus. It may thus be responsible for the extraordinarily high pathogenicity of the SARS coronavirus, compared to other viruses of this family. We describe here the three-dimensional structure of the SARS-unique domain and show that it consists of two modules with a known fold, the so-called macrodomain. Furthermore, we demonstrate that these domains bind unusual nucleic-acid structures formed by consecutive guanosine nucleotides, where four strands of nucleic acid are forming a superhelix (so-called G-quadruplexes). SUD may be involved in binding to viral or host-cell RNA bearing this peculiar structure and thereby regulate viral replication or fight the immune response of the infected host cell.¡/p¿},\n\tnumber = {5},\n\tjournal = {PLoS pathogens},\n\tauthor = {Tan, Jinzhi and Vonrhein, Clemens and Smart, Oliver S and Bricogne, Gerard and Bollati, Michela and Kusov, Yuri and Hansen, Guido and Mesters, Jeroen R and Schmidt, Christian L and Hilgenfeld, Rolf},\n\tyear = {2009},\n\tkeywords = {\\#nosource},\n\tpages = {e1000428 ST -- The SARS--Unique Domain (SUD) of SAR},\n}\n\n","author_short":["Tan, J.","Vonrhein, C.","Smart, O. S","Bricogne, G.","Bollati, M.","Kusov, Y.","Hansen, G.","Mesters, J. R","Schmidt, C. L","Hilgenfeld, R."],"key":"Tan2009-1","id":"Tan2009-1","bibbaseid":"tan-vonrhein-smart-bricogne-bollati-kusov-hansen-mesters-etal-thesarsuniquedomainsudofsarscoronaviruscontainstwomacrodomainsthatbindgquadruplexes-2009","role":"author","urls":{"Paper":"http://dx.doi.org/10.1371/journal.ppat.1000428"},"keyword":["#nosource"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/eric.larG4","dataSources":["4i5C7S78DvJNsaHyg","5L2zM5wNE5CBYNuea"],"keywords":["#nosource"],"search_terms":["sars","unique","domain","sud","sars","coronavirus","contains","two","macrodomains","bind","quadruplexes","tan","vonrhein","smart","bricogne","bollati","kusov","hansen","mesters","schmidt","hilgenfeld"],"title":"The SARS-Unique domain (SUD) of SARS coronavirus contains two macrodomains that bind g-quadruplexes","year":2009}