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==Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution==
<StructureSection load='3kvd' size='340' side='right'caption='[[3kvd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3kvd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KVD FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2w80|2w80]], [[2kc0|2kc0]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gna1870 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</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=3kvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kvd OCA], [https://pdbe.org/3kvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kvd RCSB], [https://www.ebi.ac.uk/pdbsum/3kvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kvd ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
fHbp, a highly immunogenic outer membrane protein of Neisseria meningitidis, is responsible for binding to human factor H, a multi-domain protein which is the central regulator of the alternative complement pathway. Here, the crystal structure of mature fHbp determined at 2 A resolution is presented and is compared with the structure of the same protein in complex with factor H domains 6 and 7 recently solved using X-ray techniques. While the overall protein fold is well conserved, modifications are observed mainly in the loop regions involved in the interaction, reflecting a specific adaptation of fHbp in complexing factor H with high affinity. Such a comparison has to date been impaired by the fact that fHbp models determined by NMR show remarkable differences over the entire structure.

Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086).,Cendron L, Veggi D, Girardi E, Zanotti G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):531-5. Epub 2011 Apr 20. PMID:21543855<ref>PMID:21543855</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cendron, L]]
[[Category: Girardi, E]]
[[Category: Veggi, D]]
[[Category: Zanotti, G]]
[[Category: Alternative complement pathway]]
[[Category: Antigen]]
[[Category: Lipoprotein]]
[[Category: Meningococcal vaccine]]
[[Category: Protein binding]]