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2qt4
From Proteopedia
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| - | + | ==Atomic-resolution crystal structure of the natural form of Scytovirin== | |
| - | + | <StructureSection load='2qt4' size='340' side='right'caption='[[2qt4]], [[Resolution|resolution]] 1.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2qt4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scytonema_varium Scytonema varium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QT4 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=2qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qt4 OCA], [https://pdbe.org/2qt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2qt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qt4 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/SVN_SCYVA SVN_SCYVA] Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin.<ref>PMID:12614152</ref> <ref>PMID:16647158</ref> <ref>PMID:17269926</ref> <ref>PMID:17434526</ref> | |
| - | '' | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
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| - | == | + | |
The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 A and 3.7 A, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies. | The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 A and 3.7 A, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies. | ||
| - | + | Atomic-resolution crystal structure of the antiviral lectin scytovirin.,Moulaei T, Botos I, Ziolkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A Protein Sci. 2007 Dec;16(12):2756-60. Epub 2007 Oct 26. PMID:17965185<ref>PMID:17965185</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2qt4" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Scytonema varium]] | [[Category: Scytonema varium]] | ||
| - | [[Category: Botos | + | [[Category: Botos I]] |
| - | [[Category: Dauter | + | [[Category: Dauter Z]] |
| - | [[Category: Moulaei | + | [[Category: Moulaei T]] |
| - | [[Category: Wlodawer | + | [[Category: Wlodawer A]] |
| - | [[Category: Ziolkowska | + | [[Category: Ziolkowska NE]] |
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Current revision
Atomic-resolution crystal structure of the natural form of Scytovirin
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