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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3KVD 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]] 2Å</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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6QCC2_NEIME Q6QCC2_NEIME] | |||
<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> | |||
<div class="pdbe-citations 3kvd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Cendron | [[Category: Cendron L]] | ||
[[Category: Girardi | [[Category: Girardi E]] | ||
[[Category: Veggi | [[Category: Veggi D]] | ||
[[Category: Zanotti | [[Category: Zanotti G]] | ||