1zls: Difference between revisions
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< | ==FAB 2G12 + Man4== | ||
<StructureSection load='1zls' size='340' side='right' caption='[[1zls]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zls]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZLS 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></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1om3|1om3]], [[1op3|1op3]], [[1op5|1op5]], [[1zlu|1zlu]], [[1zlv|1zlv]], [[1zlw|1zlw]]</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=1zls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zls OCA], [http://pdbe.org/1zls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zls RCSB], [http://www.ebi.ac.uk/pdbsum/1zls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zls ProSAT]</span></td></tr> | |||
</table> | |||
== 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/zl/1zls_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=1zls ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human antibody 2G12 neutralizes a broad range of HIV-1 isolates. Hence, molecular characterization of its epitope, which corresponds to a conserved cluster of oligomannoses on the viral envelope glycoprotein gp120, is a high priority in HIV vaccine design. A prior crystal structure of 2G12 in complex with Man(9)GlcNAc(2) highlighted the central importance of the D1 arm in antibody binding. To characterize the specificity of 2G12 more precisely, we performed solution-phase ELISA, carbohydrate microarray analysis, and cocrystallized Fab 2G12 with four different oligomannose derivatives (Man(4), Man(5), Man(7), and Man(8)) that compete with gp120 for binding to 2G12. Our combined studies reveal that 2G12 is capable of binding both the D1 and D3 arms of the Man(9)GlcNAc(2) moiety, which would provide more flexibility to make the required multivalent interactions between the antibody and the gp120 oligomannose cluster than thought previously. These results have important consequences for the design of immunogens to elicit 2G12-like neutralizing antibodies as a component of an HIV vaccine. | |||
Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12.,Calarese DA, Lee HK, Huang CY, Best MD, Astronomo RD, Stanfield RL, Katinger H, Burton DR, Wong CH, Wilson IA Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13372-7. Epub 2005 Sep 7. PMID:16174734<ref>PMID:16174734</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zls" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Human]] | ||
[[Category: Astronomo, R D]] | |||
[[Category: Best, M D]] | |||
== | [[Category: Burton, D R]] | ||
< | [[Category: Calarese, D A]] | ||
[[Category: | [[Category: Lee, H K]] | ||
[[Category: Astronomo, R D | [[Category: Stanfield, R L]] | ||
[[Category: Best, M D | [[Category: Wilson, I A]] | ||
[[Category: Burton, D R | [[Category: Wong, C H]] | ||
[[Category: Calarese, D A | |||
[[Category: Lee, H K | |||
[[Category: Stanfield, R L | |||
[[Category: Wilson, I A | |||
[[Category: Wong, C H | |||
[[Category: Anti-carbohydrate]] | [[Category: Anti-carbohydrate]] | ||
[[Category: Domain-swapping]] | [[Category: Domain-swapping]] | ||
[[Category: Hiv neutralizing antibody]] | [[Category: Hiv neutralizing antibody]] | ||
[[Category: Immune system]] | |||
Latest revision as of 12:21, 2 May 2018
FAB 2G12 + Man4FAB 2G12 + Man4
Structural highlights
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 PubMedHuman antibody 2G12 neutralizes a broad range of HIV-1 isolates. Hence, molecular characterization of its epitope, which corresponds to a conserved cluster of oligomannoses on the viral envelope glycoprotein gp120, is a high priority in HIV vaccine design. A prior crystal structure of 2G12 in complex with Man(9)GlcNAc(2) highlighted the central importance of the D1 arm in antibody binding. To characterize the specificity of 2G12 more precisely, we performed solution-phase ELISA, carbohydrate microarray analysis, and cocrystallized Fab 2G12 with four different oligomannose derivatives (Man(4), Man(5), Man(7), and Man(8)) that compete with gp120 for binding to 2G12. Our combined studies reveal that 2G12 is capable of binding both the D1 and D3 arms of the Man(9)GlcNAc(2) moiety, which would provide more flexibility to make the required multivalent interactions between the antibody and the gp120 oligomannose cluster than thought previously. These results have important consequences for the design of immunogens to elicit 2G12-like neutralizing antibodies as a component of an HIV vaccine. Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12.,Calarese DA, Lee HK, Huang CY, Best MD, Astronomo RD, Stanfield RL, Katinger H, Burton DR, Wong CH, Wilson IA Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13372-7. Epub 2005 Sep 7. PMID:16174734[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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