6rv6: Difference between revisions

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'''Unreleased structure'''


The entry 6rv6 is ON HOLD
==Structure of properdin lacking TSR3 based on anomalous data==
<StructureSection load='6rv6' size='340' side='right'caption='[[6rv6]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rv6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RV6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rv6 OCA], [http://pdbe.org/6rv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rv6 RCSB], [http://www.ebi.ac.uk/pdbsum/6rv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rv6 ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:[http://omim.org/entry/312060 312060]]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).<ref>PMID:8871668</ref> <ref>PMID:9710744</ref> <ref>PMID:10909851</ref> 
== Function ==
[[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 54 kDa protein properdin, also known as factor P (FP), plays a major role in the complement system through the stabilization of the alternative pathway convertases. FP circulates in the blood as cyclic dimers, trimers and tetramers, and this heterogeneity challenges detailed structural insight into the mechanism of convertase stabilization by FP. Here, the generation of an intact FP monomer and a variant monomer with the third thrombospondin repeat liberated is described. Both FP monomers were excised from recombinant full-length FP containing internal cleavage sites for TEV protease. These FP monomers could be crystallized, and complete data sets extending to 2.8 A resolution for the intact FP monomer and to 3.5 A resolution for the truncated variant were collected. The principle of specific monomer excision and domain removal by the insertion of a protease cleavage site may be broadly applicable to structural studies of oligomeric, flexible and modular proteins.


Authors:  
Crystallization and X-ray analysis of monodisperse human properdin.,Pedersen DV, Revel M, Gadeberg TAF, Andersen GR Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):0. doi:, 10.1107/S2053230X18018150. Epub 2019 Jan 23. PMID:30713161<ref>PMID:30713161</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6rv6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Andersen, G R]]
[[Category: Pedersen, D V]]
[[Category: Complement]]
[[Category: Immune system]]
[[Category: Innate immunity]]
[[Category: Protease]]
[[Category: Regulator]]

Revision as of 09:12, 21 August 2019

Structure of properdin lacking TSR3 based on anomalous dataStructure of properdin lacking TSR3 based on anomalous data

Structural highlights

6rv6 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PROP_HUMAN] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:312060]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).[1] [2] [3]

Function

[PROP_HUMAN] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.

Publication Abstract from PubMed

The 54 kDa protein properdin, also known as factor P (FP), plays a major role in the complement system through the stabilization of the alternative pathway convertases. FP circulates in the blood as cyclic dimers, trimers and tetramers, and this heterogeneity challenges detailed structural insight into the mechanism of convertase stabilization by FP. Here, the generation of an intact FP monomer and a variant monomer with the third thrombospondin repeat liberated is described. Both FP monomers were excised from recombinant full-length FP containing internal cleavage sites for TEV protease. These FP monomers could be crystallized, and complete data sets extending to 2.8 A resolution for the intact FP monomer and to 3.5 A resolution for the truncated variant were collected. The principle of specific monomer excision and domain removal by the insertion of a protease cleavage site may be broadly applicable to structural studies of oligomeric, flexible and modular proteins.

Crystallization and X-ray analysis of monodisperse human properdin.,Pedersen DV, Revel M, Gadeberg TAF, Andersen GR Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):0. doi:, 10.1107/S2053230X18018150. Epub 2019 Jan 23. PMID:30713161[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Fredrikson GN, Westberg J, Kuijper EJ, Tijssen CC, Sjoholm AG, Uhlen M, Truedsson L. Molecular characterization of properdin deficiency type III: dysfunction produced by a single point mutation in exon 9 of the structural gene causing a tyrosine to aspartic acid interchange. J Immunol. 1996 Oct 15;157(8):3666-71. PMID:8871668
  2. ↑ Fredrikson GN, Gullstrand B, Westberg J, Sjoholm AG, Uhlen M, Truedsson L. Expression of properdin in complete and incomplete deficiency: normal in vitro synthesis by monocytes in two cases with properdin deficiency type II due to distinct mutations. J Clin Immunol. 1998 Jul;18(4):272-82. PMID:9710744
  3. ↑ van den Bogaard R, Fijen CA, Schipper MG, de Galan L, Kuijper EJ, Mannens MM. Molecular characterisation of 10 Dutch properdin type I deficient families: mutation analysis and X-inactivation studies. Eur J Hum Genet. 2000 Jul;8(7):513-8. PMID:10909851 doi:10.1038/sj.ejhg.5200496
  4. ↑ Pedersen DV, Revel M, Gadeberg TAF, Andersen GR. Crystallization and X-ray analysis of monodisperse human properdin. Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):0. doi:, 10.1107/S2053230X18018150. Epub 2019 Jan 23. PMID:30713161 doi:http://dx.doi.org/10.1107/S2053230X18018150

6rv6, resolution 3.51Å

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