5d1q: Difference between revisions
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==IsdB NEAT2 bound by clone D2-06== | ==IsdB NEAT2 bound by clone D2-06== | ||
<StructureSection load='5d1q' size='340' side='right' caption='[[5d1q]], [[Resolution|resolution]] 3.22Å' scene=''> | <StructureSection load='5d1q' size='340' side='right'caption='[[5d1q]], [[Resolution|resolution]] 3.22Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d1q]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[5d1q]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Staab Staab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1Q FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1z|5d1z]], [[5d1x|5d1x]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1z|5d1z]], [[5d1x|5d1x]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">isdB, frpB, sasJ, sirH, SAB0993c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273036 STAAB])</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=5d1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1q OCA], [http://pdbe.org/5d1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1q RCSB], [http://www.ebi.ac.uk/pdbsum/5d1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1q ProSAT]</span></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=5d1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1q OCA], [http://pdbe.org/5d1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1q RCSB], [http://www.ebi.ac.uk/pdbsum/5d1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Staab]] | |||
[[Category: Deng, X]] | [[Category: Deng, X]] | ||
[[Category: Germline encoded]] | [[Category: Germline encoded]] | ||
Revision as of 13:33, 1 April 2020
IsdB NEAT2 bound by clone D2-06IsdB NEAT2 bound by clone D2-06
Structural highlights
Function[ISDB_STAAB] Seems to function as the primary receptor for hemoglobin since its inactivation inhibits the ability of S.aureus to bind hemoglobin. Binds hemoglobin in a dose-dependent way. Required for S.aureus growth using hemoglobin as the sole iron source. Also required for virulence. IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils (By similarity). Publication Abstract from PubMedStaphylococcus aureus is both an important pathogen and a human commensal. To explore this ambivalent relationship between host and microbe, we analysed the memory humoral response against IsdB, a protein involved in iron acquisition, in four healthy donors. Here we show that in all donors a heavily biased use of two immunoglobulin heavy chain germlines generated high affinity (pM) antibodies that neutralize the two IsdB NEAT domains, IGHV4-39 for NEAT1 and IGHV1-69 for NEAT2. In contrast to the typical antibody/antigen interactions, the binding is primarily driven by the germline-encoded hydrophobic CDRH-2 motifs of IGHV1-69 and IGHV4-39, with a binding mechanism nearly identical for each antibody derived from different donors. Our results suggest that IGHV1-69 and IGHV4-39, while part of the adaptive immune system, may have evolved under selection pressure to encode a binding motif innately capable of recognizing and neutralizing a structurally conserved protein domain involved in pathogen iron acquisition. Germline-encoded neutralization of a Staphylococcus aureus virulence factor by the human antibody repertoire.,Yeung YA, Foletti D, Deng X, Abdiche Y, Strop P, Glanville J, Pitts S, Lindquist K, Sundar PD, Sirota M, Hasa-Moreno A, Pham A, Melton Witt J, Ni I, Pons J, Shelton D, Rajpal A, Chaparro-Riggers J Nat Commun. 2016 Nov 18;7:13376. doi: 10.1038/ncomms13376. PMID:27857134[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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