View source for 2k7x


==solution structure of C-terminal domain of SARS-CoV main protease==
<StructureSection load='2k7x' size='340' side='right'caption='[[2k7x]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2k7x]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=2k7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7x OCA], [https://pdbe.org/2k7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7x RCSB], [https://www.ebi.ac.uk/pdbsum/2k7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7x ProSAT]</span></td></tr>
</table>
== Function ==
[[https://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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k7x ConSurf].
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== Publication Abstract from PubMed ==
SARS 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<ref>PMID:19319935</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sars coronavirus sino1-11]]
[[Category: Xia, B]]
[[Category: Zhong, N]]
[[Category: C-terminal domain]]
[[Category: Hydrolase]]
[[Category: Main protease]]
[[Category: Solution structure]]