2k7x: Difference between revisions
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<StructureSection load='2k7x' size='340' side='right' caption='[[2k7x]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | <StructureSection load='2k7x' size='340' side='right' caption='[[2k7x]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2k7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus_sino1-11 Sars coronavirus sino1-11]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7X FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7x RCSB], [http://www.ebi.ac.uk/pdbsum/2k7x PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7x OCA], [http://pdbe.org/2k7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k7x RCSB], [http://www.ebi.ac.uk/pdbsum/2k7x PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2k7x" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus sino1-11]] | ||
[[Category: Xia, B]] | [[Category: Xia, B]] | ||
[[Category: Zhong, N]] | [[Category: Zhong, N]] | ||
Revision as of 23:35, 10 September 2015
solution structure of C-terminal domain of SARS-CoV main proteasesolution structure of C-terminal domain of SARS-CoV main protease
Structural highlights
Function[Q6JH47_CVHSA] Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).[SAAS:SAAS008740_004_014545] Nsp9 is a ssRNA-binding protein (By similarity).[SAAS:SAAS008740_004_001449] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSARS coronavirus main protease (M(pro)) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. We have reported that both the M(pro) C-terminal domain alone (M(pro)-C) and the N-finger deletion mutant of M(pro) (M(pro)-Delta7) exist as a stable dimer and a stable monomer (Zhong et al., J Virol 2008; 82:4227-4234). Here, we report structures of both M(pro)-C monomer and dimer. The structure of the M(pro)-C monomer is almost identical to that of the C-terminal domain in the crystal structure of M(pro). Interestingly, the M(pro)-C dimer structure is characterized by 3D domain-swapping, in which the first helices of the two protomers are interchanged and each is enwrapped by four other helices from the other protomer. Each folding subunit of the M(pro)-C domain-swapped dimer still has the same general fold as that of the M(pro)-C monomer. This special dimerization elucidates the structural basis for the observation that there is no exchange between monomeric and dimeric forms of M(pro)-C and M(pro)-Delta7. C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer.,Zhong N, Zhang S, Xue F, Kang X, Zou P, Chen J, Liang C, Rao Z, Jin C, Lou Z, Xia B Protein Sci. 2009 Apr;18(4):839-44. PMID:19319935[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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