6efa: Difference between revisions
New page: '''Unreleased structure''' The entry 6efa is ON HOLD Authors: Iverson, T.M. Description: GspB Siglec domain Category: Unreleased Structures Category: Iverson, T.M |
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The | ==GspB Siglec + Unique domains== | ||
<StructureSection load='6efa' size='340' side='right'caption='[[6efa]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6efa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_gordonii Streptococcus gordonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EFA 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]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6efa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efa OCA], [https://pdbe.org/6efa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6efa RCSB], [https://www.ebi.ac.uk/pdbsum/6efa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6efa ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GSPB_STRGN GSPB_STRGN] Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA.<ref>PMID:21765814</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire. | |||
Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.,Bensing BA, Stubbs HE, Agarwal R, Yamakawa I, Luong K, Solakyildirim K, Yu H, Hadadianpour A, Castro MA, Fialkowski KP, Morrison KM, Wawrzak Z, Chen X, Lebrilla CB, Baudry J, Smith JC, Sullam PM, Iverson TM Nat Commun. 2022 May 18;13(1):2753. doi: 10.1038/s41467-022-30509-y. PMID:35585145<ref>PMID:35585145</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Iverson | <div class="pdbe-citations 6efa" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus gordonii]] | |||
[[Category: Iverson TM]] | |||
Latest revision as of 13:08, 22 May 2024
GspB Siglec + Unique domainsGspB Siglec + Unique domains
Structural highlights
FunctionGSPB_STRGN Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA.[1] Publication Abstract from PubMedBacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire. Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.,Bensing BA, Stubbs HE, Agarwal R, Yamakawa I, Luong K, Solakyildirim K, Yu H, Hadadianpour A, Castro MA, Fialkowski KP, Morrison KM, Wawrzak Z, Chen X, Lebrilla CB, Baudry J, Smith JC, Sullam PM, Iverson TM Nat Commun. 2022 May 18;13(1):2753. doi: 10.1038/s41467-022-30509-y. PMID:35585145[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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