3kvd: Difference between revisions
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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]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kvd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KVD FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w80|2w80]], [[2kc0|2kc0]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gna1870 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis])</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=3kvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kvd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kvd RCSB], [http://www.ebi.ac.uk/pdbsum/3kvd PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Cendron, L | [[Category: Cendron, L]] | ||
[[Category: Girardi, E | [[Category: Girardi, E]] | ||
[[Category: Veggi, D | [[Category: Veggi, D]] | ||
[[Category: Zanotti, G | [[Category: Zanotti, G]] | ||
[[Category: Alternative complement pathway]] | [[Category: Alternative complement pathway]] | ||
[[Category: Antigen]] | [[Category: Antigen]] | ||
Revision as of 17:04, 18 December 2014
Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution
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