Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module
Identifieur interne : 001156 ( Main/Exploration ); précédent : 001155; suivant : 001157Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module
Auteurs : Chao-Cheng Cho ; Meng-Hsuan Lin ; Chien-Ying Chuang ; Chun-Hua HsuSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2016.
Descripteurs français
- KwdFr :
- Adénosine diphosphate ribose (métabolisme), Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Données de séquences moléculaires, Liaison aux protéines, Protéines virales (), Protéines virales (métabolisme), Sites de fixation, Séquence d'acides aminés.
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Proteins.
- chemical , metabolism : Adenosine Diphosphate Ribose, Viral Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- metabolism : Middle East Respiratory Syndrome Coronavirus.
- Amino Acid Sequence, Binding Sites, Molecular Sequence Data, Protein Binding.
Abstract
The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-Å resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the α1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.
Url:
DOI: 10.1074/jbc.M115.700542
PubMed: 26740631
PubMed Central: 4777827
Affiliations:
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(MERS-CoV) Is an Efficient ADP-ribose Binding Module</title><author><name sortKey="Cho, Chao Cheng" sort="Cho, Chao Cheng" uniqKey="Cho C" first="Chao-Cheng" last="Cho">Chao-Cheng Cho</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lin, Meng Hsuan" sort="Lin, Meng Hsuan" uniqKey="Lin M" first="Meng-Hsuan" last="Lin">Meng-Hsuan Lin</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Chuang, Chien Ying" sort="Chuang, Chien Ying" uniqKey="Chuang C" first="Chien-Ying" last="Chuang">Chien-Ying Chuang</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Hsu, Chun Hua" sort="Hsu, Chun Hua" uniqKey="Hsu C" first="Chun-Hua" last="Hsu">Chun-Hua Hsu</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate Ribose (metabolism)</term><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term><term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adénosine diphosphate ribose (métabolisme)</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Protéines virales ()</term><term>Protéines virales (métabolisme)</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate Ribose</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adénosine diphosphate ribose</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Molecular Sequence Data</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Protéines virales</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV)
encodes the conserved macro domain within non-structural protein 3. However, the
precise biochemical function and structure of the macro domain is unclear. Using
differential scanning fluorimetry and isothermal titration calorimetry, we
characterized the MERS-CoV macro domain as a more efficient adenosine
diphosphate (ADP)-ribose binding module than macro domains from other CoVs.
Furthermore, the crystal structure of the MERS-CoV macro domain was determined
at 1.43-Å resolution in complex with ADP-ribose. Comparison of macro
domains from MERS-CoV and other human CoVs revealed structural differences in
the α1 helix alters how the conserved Asp-20 interacts with ADP-ribose and
may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose.
This study provides structural and biophysical bases to further evaluate the
role of the MERS-CoV macro domain in the host response via ADP-ribose binding
but also as a potential target for drug design.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Hui, D X0a S" uniqKey="Hui D">D.
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