|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6q1g' size='340' side='right'caption='[[6q1g]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6q1g' size='340' side='right'caption='[[6q1g]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6q1g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q1G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q1G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.75Å</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=6q1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q1g OCA], [http://pdbe.org/6q1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q1g RCSB], [http://www.ebi.ac.uk/pdbsum/6q1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q1g ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6q1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q1g OCA], [https://pdbe.org/6q1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q1g RCSB], [https://www.ebi.ac.uk/pdbsum/6q1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q1g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 16: |
Line 17: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6q1g" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6q1g" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Antibody 3D structures|Antibody 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Harrison, S C]] | + | [[Category: Harrison SC]] |
| - | [[Category: McCarthy, K R]] | + | [[Category: McCarthy KR]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Affinity maturation of the B cell antigen receptor (BCR) is a conserved and crucial component of the adaptive immune response. BCR lineages, inferred from paired heavy- and light-chain sequences of rearranged Ig genes from multiple descendants of the same naive B cell precursor (the lineages' unmutated common ancestor, "UCA"), make it possible to reconstruct the underlying somatic evolutionary history. We present here an extensive structural and biophysical analysis of a lineage of BCRs directed against the receptor binding site (RBS) of subtype H1 influenza virus hemagglutinin (HA). The lineage includes 8 antibodies detected directly by sequencing, 3 in 1 principal branch and 5 in the other. When bound to HA, the heavy-chain third complementarity determining region (HCDR3) fits with an invariant pose into the RBS, but in each of the 2 branches, the rest of the Fab reorients specifically, from its position in the HA-bound UCA, about a hinge at the base of HCDR3. New contacts generated by the reorientation compensate for contacts lost as the H1 HA mutated during the time between the donor's initial exposure and the vaccination that preceded sampling. Our data indicate that a "pluripotent" naive response differentiated, in each branch, into 1 of its possible alternatives. This property of naive BCRs and persistence of multiple branches of their progeny lineages can offer broader protection from evolving pathogens than can a single, linear pathway of somatic mutation.
Affinity maturation in a human humoral response to influenza hemagglutinin.,McCarthy KR, Raymond DD, Do KT, Schmidt AG, Harrison SC Proc Natl Acad Sci U S A. 2019 Dec 16. pii: 1915620116. doi:, 10.1073/pnas.1915620116. PMID:31843892[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McCarthy KR, Raymond DD, Do KT, Schmidt AG, Harrison SC. Affinity maturation in a human humoral response to influenza hemagglutinin. Proc Natl Acad Sci U S A. 2019 Dec 16. pii: 1915620116. doi:, 10.1073/pnas.1915620116. PMID:31843892 doi:http://dx.doi.org/10.1073/pnas.1915620116
|
