1om3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==FAB 2G12 unliganded== | ==FAB 2G12 unliganded== | ||
<StructureSection load='1om3' size='340' side='right' caption='[[1om3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1om3' size='340' side='right' caption='[[1om3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[1om3]] is a 4 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=1OM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OM3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1om3]] is a 4 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=1OM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OM3 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1op3|1op3]], [[1op5|1op5]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1op3|1op3]], [[1op5|1op5]]</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=1om3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1om3 OCA], [http://pdbe.org/1om3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1om3 RCSB], [http://www.ebi.ac.uk/pdbsum/1om3 PDBsum]</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=1om3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1om3 OCA], [http://pdbe.org/1om3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1om3 RCSB], [http://www.ebi.ac.uk/pdbsum/1om3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1om3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 14: | Line 15: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1om3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 27: | Line 28: | ||
==See Also== | ==See Also== | ||
*[[ | *[[3D structures of antibody|3D structures of antibody]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:59, 1 November 2017
FAB 2G12 unligandedFAB 2G12 unliganded
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 human immunodeficiency virus type 1 (HIV-1) isolates by binding an unusually dense cluster of carbohydrate moieties on the "silent" face of the gp120 envelope glycoprotein. Crystal structures of Fab 2G12 and its complexes with the disaccharide Manalpha1-2Man and with the oligosaccharide Man9GlcNAc2 revealed that two Fabs assemble into an interlocked VH domain-swapped dimer. Further biochemical, biophysical, and mutagenesis data strongly support a Fab-dimerized antibody as the prevalent form that recognizes gp120. The extraordinary configuration of this antibody provides an extended surface, with newly described binding sites, for multivalent interaction with a conserved cluster of oligomannose type sugars on the surface of gp120. The unique interdigitation of Fab domains within an antibody uncovers a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition.,Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, Kunert R, Zhu P, Wormald MR, Stanfield RL, Roux KH, Kelly JW, Rudd PM, Dwek RA, Katinger H, Burton DR, Wilson IA Science. 2003 Jun 27;300(5628):2065-71. PMID:12829775[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||