|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of a complex of griffithsin with 6alpha-mannobiose== | | ==Crystal structure of a complex of griffithsin with 6alpha-mannobiose== |
| - | <StructureSection load='2hyq' size='340' side='right' caption='[[2hyq]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2hyq' size='340' side='right'caption='[[2hyq]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hyq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Griffithsia Griffithsia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hyq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Griffithsia Griffithsia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HYQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gty|2gty]], [[2guc|2guc]], [[2gud|2gud]], [[2gue|2gue]], [[2gux|2gux]], [[2hyr|2hyr]]</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=2hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyq OCA], [https://pdbe.org/2hyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hyq RCSB], [https://www.ebi.ac.uk/pdbsum/2hyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyq ProSAT]</span></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=2hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyq OCA], [http://pdbe.org/2hyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hyq RCSB], [http://www.ebi.ac.uk/pdbsum/2hyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GRFIN_GRISQ GRFIN_GRISQ] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/2hyq_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/2hyq_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 33: |
Line 34: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Griffithsia]] | | [[Category: Griffithsia]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Ziolkowska, N E]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Domain swapping]] | + | [[Category: Ziolkowska NE]] |
| - | [[Category: Griffithsin]]
| + | |
| - | [[Category: Hiv]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Mannose binding]]
| + | |
| - | [[Category: Sar]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
GRFIN_GRISQ
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 PubMed
The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X-ray crystallography, isothermal titration calorimetry, and molecular modeling. The structures of complexes of griffithsin with 1-->6alpha-mannobiose and with maltose were solved and refined at the resolution of 2.0 and 1.5 A, respectively. The thermodynamic parameters of binding of 1-->6alpha-mannobiose, maltose, and mannose to griffithsin were determined. Binding profiles of 1-->6alpha-mannobiose and mannose were similar with Kd values of 83.3 microM and 102 microM, respectively. The binding of maltose to griffithsin was significantly weaker, with a fourfold lower affinity (Kd = 394 microM). In all cases the binding at 30 degrees C was entropically rather than enthalpically driven. On the basis of the experimental crystal structures, as well as on previously determined structures of complexes with monosaccharides, it was possible to create a model of a tridentate complex of griffithsin with Man9GlcNAc2, a high mannose oligosaccharide commonly found on the surface of viral glycoproteins. All shorter oligomannoses could be modeled only as bidentate or monodentate complexes with griffithsin. The ability to mediate tight multivalent and multisite interactions with high-mannose oligosaccharides helps to explain the potent antiviral activity of griffithsin.
Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin.,Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A Proteins. 2007 May 15;67(3):661-70. PMID:17340634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A. Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin. Proteins. 2007 May 15;67(3):661-70. PMID:17340634 doi:10.1002/prot.21336
|
