3phq: Difference between revisions
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[[ | ==Crystal structure of S64-4 in complex with KDO== | ||
<StructureSection load='3phq' size='340' side='right' caption='[[3phq]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3phq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PHQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pho|3pho]]</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=3phq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3phq RCSB], [http://www.ebi.ac.uk/pdbsum/3phq PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of the antigen-binding fragment from the monoclonal antibody S64-4 in complex with a pentasaccharide bisphosphate fragment from chlamydial lipopolysaccharide has been determined by x-ray diffraction to 2.6 A resolution. Like the well-characterized antibody S25-2, S64-4 displays a pocket formed by the residues of germline sequence corresponding to the heavy and light chain V genes that binds the terminal Kdo residue of the antigen; however, while S64-4 shares the same heavy chain V gene as S25-2 it has a different light chain V gene. The new V(L) gene codes for a combining site that displays greater affinity, different specificity, and allows a novel antigen conformation that brings a greater number of antigen residues into the combining site than possible in S25-2. Further, while antibodies in the S25-2 family use CDR H3 to discriminate among antigens, S64-4 achieves its specificity via the new light chain V gene and resulting change in antigen conformation. These structures reveal an intriguing parallel strategy where two different combinations of germline-coded V genes can act as starting points for the generation of germline antibodies against chlamydial antigens, and shows how anti-carbohydrate antibodies can exploit the conformational flexibility of this class of antigens to achieve high affinity and specificity independently of CDR H3. | |||
Structural insights into parallel strategies for germline antibody recognition of LPS from Chlamydia.,Evans DW, Muller-Loennies S, Brooks CL, Brade L, Kosma P, Brade H, Evans SV Glycobiology. 2011 May 4. PMID:21543444<ref>PMID:21543444</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Antibody|Antibody]] | *[[Antibody|Antibody]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Evans, D W | [[Category: Evans, D W]] | ||
[[Category: Evans, S V | [[Category: Evans, S V]] | ||
[[Category: Antibody]] | [[Category: Antibody]] | ||
[[Category: Carbohydrate]] | [[Category: Carbohydrate]] | ||
Revision as of 11:58, 9 December 2014
Crystal structure of S64-4 in complex with KDO
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