2y07: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y07 OCA], [https://pdbe.org/2y07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y07 RCSB], [https://www.ebi.ac.uk/pdbsum/2y07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y07 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=2y07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y07 OCA], [https://pdbe.org/2y07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y07 RCSB], [https://www.ebi.ac.uk/pdbsum/2y07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y07 ProSAT]</span></td></tr>
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2y07" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 10:11, 1 May 2024

CRYSTAL STRUCTURE ANALYSIS OF THE ANTI-(4-HYDROXY-3-NITROPHENYL) - ACETYL MURINE GERMLINE MONOCLONAL ANTIBODY BBE6.12H3 FAB FRAGMENT IN COMPLEX WITH A PHAGE DISPLAY DERIVED DODECAPEPTIDE PPYPAWHAPGNICRYSTAL STRUCTURE ANALYSIS OF THE ANTI-(4-HYDROXY-3-NITROPHENYL) - ACETYL MURINE GERMLINE MONOCLONAL ANTIBODY BBE6.12H3 FAB FRAGMENT IN COMPLEX WITH A PHAGE DISPLAY DERIVED DODECAPEPTIDE PPYPAWHAPGNI

Structural highlights

2y07 is a 3 chain structure with sequence from Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

2y07, resolution 2.40Å

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