View source for 4k12


==Structural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae==
<StructureSection load='4k12' size='340' side='right'caption='[[4k12]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4k12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K12 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]] 1.079&#8491;</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=4k12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k12 OCA], [https://pdbe.org/4k12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k12 RCSB], [https://www.ebi.ac.uk/pdbsum/4k12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k12 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Many human pathogens have strict host specificity, which affects not only their epidemiology but also development of animal models and vaccines. Complement factor H (FH) is recruited to pneumococcal cell surface in a human-specific manner via the N-terminal domain of the pneumococcal protein virulence factor CbpA (CbpAN). FH recruitment enables Streptococcus pneumoniae to evade surveillance by human complement system and contributes to pneumococcal host specificity. The molecular determinants of host specificity of complement evasion are unknown. Here we show that a single human FH domain is sufficient for tight binding of CbpAN, present the crystal structure of the complex, and identify the critical structural determinants for host-specific FH recruitment. The results offer new approaches to development of better animal models for pneumococcal infection and redesign of the virulence factor for pneumococcal vaccine development, and reveal how FH recruitment can serve as a mechanism for both pneumococcal complement evasion and adherence.

Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae.,Achila D, Liu A, Banerjee R, Li Y, Martinez-Hackert E, Zhang JR, Yan H Biochem J. 2014 Oct 21. PMID:25330773<ref>PMID:25330773</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4k12" style="background-color:#fffaf0;"></div>

==See Also==
*[[Complement factor 3D structures|Complement factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Achila D]]
[[Category: Banerjee R]]
[[Category: Li Y]]
[[Category: Liu A]]
[[Category: Martinez-Hackert E]]
[[Category: Yan H]]