4bl4: Difference between revisions
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New page: '''Unreleased structure''' The entry 4bl4 is ON HOLD until Paper Publication Authors: Caesar, J.J.E., Wallich, R., Kraiczy, P., Zipfel, P.F., Lea, S.M. Description: Further structural ... |
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==Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.== | |||
<StructureSection load='4bl4' size='340' side='right'caption='[[4bl4]], [[Resolution|resolution]] 4.06Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bl4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_ZS7 Borreliella burgdorferi ZS7]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4atr 4atr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BL4 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]] 4.06Å</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=4bl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bl4 OCA], [https://pdbe.org/4bl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bl4 RCSB], [https://www.ebi.ac.uk/pdbsum/4bl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bl4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H3BZN5_BORBZ A0A0H3BZN5_BORBZ] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators. | |||
Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.,Caesar JJ, Wallich R, Kraiczy P, Zipfel PF, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):629-33. doi: , 10.1107/S1744309113012748. Epub 2013 May 23. PMID:23722839<ref>PMID:23722839</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bl4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Complement Regulator-Acquiring Surface Protein|Complement Regulator-Acquiring Surface Protein]] | |||
*[[Complement regulator-acquiring surface protein|Complement regulator-acquiring surface protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Borreliella burgdorferi ZS7]] | |||
[[Category: Large Structures]] | |||
[[Category: Caesar JJE]] | |||
[[Category: Kraiczy P]] | |||
[[Category: Lea SM]] | |||
[[Category: Wallich R]] | |||
[[Category: Zipfel PF]] | |||
Latest revision as of 14:53, 20 December 2023
Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.
Structural highlights
FunctionPublication Abstract from PubMedBorrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators. Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.,Caesar JJ, Wallich R, Kraiczy P, Zipfel PF, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):629-33. doi: , 10.1107/S1744309113012748. Epub 2013 May 23. PMID:23722839[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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