3pho: Difference between revisions
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==Crystal structure of S64-4 in complex with PSBP== | |||
<StructureSection load='3pho' size='340' side='right'caption='[[3pho]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=Z9M:2-AMINO-2-DEOXY-4-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>Z9M</scene></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=3pho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pho OCA], [https://pdbe.org/3pho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pho RCSB], [https://www.ebi.ac.uk/pdbsum/3pho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pho ProSAT]</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> | |||
<div class="pdbe-citations 3pho" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Evans DW]] | |||
[[Category: Evans SV]] | |||
Latest revision as of 09:05, 17 October 2024
Crystal structure of S64-4 in complex with PSBPCrystal structure of S64-4 in complex with PSBP
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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