2k7x: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. 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> | <table><tr><td colspan='2'>[[2k7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. 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><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://www.rcsb.org/pdb/explore.do?structureId=2k7x RCSB], [http://www.ebi.ac.uk/pdbsum/2k7x PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q6JH47_CVHSA 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Xia, B | [[Category: Xia, B]] | ||
[[Category: Zhong, N | [[Category: Zhong, N]] | ||
[[Category: C-terminal domain]] | [[Category: C-terminal domain]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Main protease]] | [[Category: Main protease]] | ||
[[Category: Solution structure]] | [[Category: Solution structure]] | ||
Revision as of 08:49, 25 December 2014
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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