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| - | {{Seed}} | |
| - | [[Image:2qt4.png|left|200px]] | |
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| - | <!--
| + | ==Atomic-resolution crystal structure of the natural form of Scytovirin== |
| - | The line below this paragraph, containing "STRUCTURE_2qt4", creates the "Structure Box" on the page.
| + | <StructureSection load='2qt4' size='340' side='right'caption='[[2qt4]], [[Resolution|resolution]] 1.30Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <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> |
| - | or leave the SCENE parameter empty for the default display. | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</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> |
| - | {{STRUCTURE_2qt4| PDB=2qt4 | SCENE= }}
| + | </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 == |
| | + | 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 natural form of Scytovirin===
| + | 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> |
| | | | |
| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_17965185}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 2qt4" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 17965185 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_17965185}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QT4 OCA].
| + | [[Category: Scytonema varium]] |
| - | | + | [[Category: Botos I]] |
| - | ==Reference== | + | [[Category: Dauter Z]] |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17965185 17965185]
| + | [[Category: Moulaei T]] |
| - | [[Category: Botos, I.]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Dauter, Z.]] | + | [[Category: Ziolkowska NE]] |
| - | [[Category: Moulaei, T.]] | + | |
| - | [[Category: Wlodawer, A.]] | + | |
| - | [[Category: Ziolkowska, N E.]] | + | |
| - | [[Category: Lectin]] | + | |
| - | [[Category: Sugar binding protein]] | + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:52:51 2008''
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
Publication Abstract from PubMed
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bokesch HR, O'Keefe BR, McKee TC, Pannell LK, Patterson GM, Gardella RS, Sowder RC 2nd, Turpin J, Watson K, Buckheit RW Jr, Boyd MR. A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. Biochemistry. 2003 Mar 11;42(9):2578-84. doi: 10.1021/bi0205698. PMID:12614152 doi:http://dx.doi.org/10.1021/bi0205698
- ↑ Xiong C, O'Keefe BR, Byrd RA, McMahon JB. Potent anti-HIV activity of scytovirin domain 1 peptide. Peptides. 2006 Jul;27(7):1668-75. doi: 10.1016/j.peptides.2006.03.018. Epub 2006 , May 2. PMID:16647158 doi:http://dx.doi.org/10.1016/j.peptides.2006.03.018
- ↑ Ratner DM, Seeberger PH. Carbohydrate microarrays as tools in HIV glycobiology. Curr Pharm Des. 2007;13(2):173-83. doi: 10.2174/138161207779313650. PMID:17269926 doi:http://dx.doi.org/10.2174/138161207779313650
- ↑ McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA. The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors. J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:17434526 doi:http://dx.doi.org/S0022-2836(07)00371-3
- ↑ Moulaei T, Botos I, Ziolkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A. Atomic-resolution crystal structure of the antiviral lectin scytovirin. Protein Sci. 2007 Dec;16(12):2756-60. Epub 2007 Oct 26. PMID:17965185 doi:ps.073157507
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