4a6y: Difference between revisions
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The | ==CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-(4-HYDROXY-3-NITROPHENYL) -ACETYL MURINE GERMLINE ANTIBODY BBE6.12H3== | ||
<StructureSection load='4a6y' size='340' side='right'caption='[[4a6y]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a6y]] is a 4 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=4A6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A6Y 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]] 2.9Å</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=4a6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6y OCA], [https://pdbe.org/4a6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a6y RCSB], [https://www.ebi.ac.uk/pdbsum/4a6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a6y ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mechanistic basis for efficient combating of the infinite range of foreign Ags by the limited repertoire of naive Abs expressed on primary B cell surfaces during their first encounter was addressed through elegantly designed crystallographic analyses. Resolution of the discrepancy arising from the limited number of possible germline Ab receptors on primary B cells for recognizing the unlimited pool of possible Ags has been attempted by invoking the degenerate recognition potential of the germline Abs. Structural analyses of germline mAb BBE6.12H3 in an Ag-free state, as well as bound to four different peptide Ags, established the correlation of its degenerate specificity with conformational versatility of the paratope. Six distinct paratope topologies observed for a single germline mAb provided a quantitative description of the primary Ag recognition repertoire at the tertiary structural level. Each of the four different peptide Ags was bound specifically to a distinct conformation of the paratope, which was also different from that of the Ag-free states of the same germline mAb. A minimal conserved motif in the pristine Ag-combining site essential for multispecificity and Ag binding-mediated change in the elbow angle of Fab was also discernible. It is proposed that the generation of a primary Ab repertoire involves large, yet finite, germline Ab clones, each capable of adopting discrete conformations, which in turn exhibit diverse binding modes. | |||
Structural elucidation of the mechanistic basis of degeneracy in the primary humoral response.,Khan T, Salunke DM J Immunol. 2012 Feb 15;188(4):1819-27. Epub 2012 Jan 20. PMID:22266283<ref>PMID:22266283</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a6y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Khan T]] | |||
[[Category: Salunke DM]] | |||
Latest revision as of 14:20, 20 December 2023
CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-(4-HYDROXY-3-NITROPHENYL) -ACETYL MURINE GERMLINE ANTIBODY BBE6.12H3CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-(4-HYDROXY-3-NITROPHENYL) -ACETYL MURINE GERMLINE ANTIBODY BBE6.12H3
Structural highlights
Publication Abstract from PubMedThe mechanistic basis for efficient combating of the infinite range of foreign Ags by the limited repertoire of naive Abs expressed on primary B cell surfaces during their first encounter was addressed through elegantly designed crystallographic analyses. Resolution of the discrepancy arising from the limited number of possible germline Ab receptors on primary B cells for recognizing the unlimited pool of possible Ags has been attempted by invoking the degenerate recognition potential of the germline Abs. Structural analyses of germline mAb BBE6.12H3 in an Ag-free state, as well as bound to four different peptide Ags, established the correlation of its degenerate specificity with conformational versatility of the paratope. Six distinct paratope topologies observed for a single germline mAb provided a quantitative description of the primary Ag recognition repertoire at the tertiary structural level. Each of the four different peptide Ags was bound specifically to a distinct conformation of the paratope, which was also different from that of the Ag-free states of the same germline mAb. A minimal conserved motif in the pristine Ag-combining site essential for multispecificity and Ag binding-mediated change in the elbow angle of Fab was also discernible. It is proposed that the generation of a primary Ab repertoire involves large, yet finite, germline Ab clones, each capable of adopting discrete conformations, which in turn exhibit diverse binding modes. Structural elucidation of the mechanistic basis of degeneracy in the primary humoral response.,Khan T, Salunke DM J Immunol. 2012 Feb 15;188(4):1819-27. Epub 2012 Jan 20. PMID:22266283[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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