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| | <StructureSection load='3ab0' size='340' side='right'caption='[[3ab0]], [[Resolution|resolution]] 3.09Å' scene=''> | | <StructureSection load='3ab0' size='340' side='right'caption='[[3ab0]], [[Resolution|resolution]] 3.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ab0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_'34f2_(nmrc)' Bacillus anthracis '34f2 (nmrc)'] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AB0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ab0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._'34F2_(NMRC)' Bacillus anthracis str. '34F2 (NMRC)'] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AB0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z5w|2z5w]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.09Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bclA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=526966 Bacillus anthracis '34F2 (NMRC)']), 35G-5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3ab0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ab0 OCA], [https://pdbe.org/3ab0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ab0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ab0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ab0 ProSAT]</span></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=3ab0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ab0 OCA], [https://pdbe.org/3ab0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ab0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ab0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ab0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q83WB0_BACAN Q83WB0_BACAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Streltsov, V A]] | + | [[Category: Streltsov VA]] |
| - | [[Category: Anthrax]]
| + | |
| - | [[Category: Exosporium]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Scfv complex]]
| + | |
| - | [[Category: Tbcla]]
| + | |
| Structural highlights
Function
Q83WB0_BACAN
Publication Abstract from PubMed
One method of laboratory- or field-based testing for anthrax is detection of Bacillus anthracis spores by high-affinity, high specificity binding reagents. From a pool of monoclonal antibodies, we selected one such candidate (A4D11) with high affinity for tBclA, a truncated version of the B. anthracis exosporium protein BclA. Kinetic analysis utilising both standard and kinetic titration on a Biacore biosensor indicated antibody affinities in the 300 pM range for recombinant tBclA, and the A4D11 antibody was also re-formatted into scFv configuration with no loss of affinity. However, assays against B. anthracis and related Bacilli species showed limited binding of intact spores as well as significant cross-reactivity between species. These results were rationalized by determination of the three-dimensional crystallographic structure of the scFv-tBclA complex. A4D11 binds the side of the tBclA trimer, contacting a face of the antigen normally packed against adjacent trimers within the exosporium structure; this inter-spore interface is highly conserved between Bacilli species. Our results indicate the difficulty of generating a high-affinity antibody to differentiate between the highly conserved spore structures of closely related species, but suggest the possibility of future structure-based antibody design for this difficult target.
Isolation, kinetic analysis, and structural characterization of an antibody targeting the Bacillus anthracis major spore surface protein BclA.,Nuttall SD, Wilkins ML, Streltsov VA, Pontes-Braz L, Dolezal O, Tran H, Liu CQ Proteins. 2011 Apr;79(4):1306-17. doi: 10.1002/prot.22971. Epub 2011 Feb 14. PMID:21322055[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nuttall SD, Wilkins ML, Streltsov VA, Pontes-Braz L, Dolezal O, Tran H, Liu CQ. Isolation, kinetic analysis, and structural characterization of an antibody targeting the Bacillus anthracis major spore surface protein BclA. Proteins. 2011 Apr;79(4):1306-17. doi: 10.1002/prot.22971. Epub 2011 Feb 14. PMID:21322055 doi:http://dx.doi.org/10.1002/prot.22971
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