4r2g: Difference between revisions
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''' | ==Crystal Structure of PGT124 Fab bound to HIV-1 JRCSF gp120 core and to CD4== | ||
<StructureSection load='4r2g' size='340' side='right' caption='[[4r2g]], [[Resolution|resolution]] 3.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r2g]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R2G FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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">[[4r26|4r26]]</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=4r2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r2g RCSB], [http://www.ebi.ac.uk/pdbsum/4r2g PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of broadly neutralizing antibodies (Abs) has evolved common and distinct structural features to counter the glycan shield and interact with both glycan and protein components of HIV Env. The inferred germline antibody already harbors potential binding pockets for a glycan and a short protein segment. Affinity maturation then leads to divergent evolutionary branches that either focus on a single glycan and protein segment (e.g., Ab PGT124) or engage multiple glycans (e.g., Abs PGT121-123). Furthermore, other surrounding glycans are avoided by selecting an appropriate initial antibody shape that prevents steric hindrance. Such molecular recognition lessons are important for engineering proteins that can recognize or accommodate glycans. | |||
Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies.,Garces F, Sok D, Kong L, McBride R, Kim HJ, Saye-Francisco KF, Julien JP, Hua Y, Cupo A, Moore JP, Paulson JC, Ward AB, Burton DR, Wilson IA Cell. 2014 Sep 25;159(1):69-79. doi: 10.1016/j.cell.2014.09.009. PMID:25259921<ref>PMID:25259921</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Garces, F.]] | |||
[[Category: Wilson, I A.]] | |||
[[Category: Anti-hiv antibody]] | |||
[[Category: Gp120]] | |||
[[Category: Igg]] | |||
[[Category: Immune system]] | |||
[[Category: Protein-protein complex]] | |||
Revision as of 10:37, 8 October 2014
Crystal Structure of PGT124 Fab bound to HIV-1 JRCSF gp120 core and to CD4Crystal Structure of PGT124 Fab bound to HIV-1 JRCSF gp120 core and to CD4
Structural highlights
Publication Abstract from PubMedThe HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of broadly neutralizing antibodies (Abs) has evolved common and distinct structural features to counter the glycan shield and interact with both glycan and protein components of HIV Env. The inferred germline antibody already harbors potential binding pockets for a glycan and a short protein segment. Affinity maturation then leads to divergent evolutionary branches that either focus on a single glycan and protein segment (e.g., Ab PGT124) or engage multiple glycans (e.g., Abs PGT121-123). Furthermore, other surrounding glycans are avoided by selecting an appropriate initial antibody shape that prevents steric hindrance. Such molecular recognition lessons are important for engineering proteins that can recognize or accommodate glycans. Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies.,Garces F, Sok D, Kong L, McBride R, Kim HJ, Saye-Francisco KF, Julien JP, Hua Y, Cupo A, Moore JP, Paulson JC, Ward AB, Burton DR, Wilson IA Cell. 2014 Sep 25;159(1):69-79. doi: 10.1016/j.cell.2014.09.009. PMID:25259921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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