2o39: Difference between revisions

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<StructureSection load='2o39' size='340' side='right'caption='[[2o39]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='2o39' size='340' side='right'caption='[[2o39]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2o39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ade1p Ade1p] and [https://en.wikipedia.org/wiki/Human Human]. The December 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O39 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2o39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_adenovirus_11p Human adenovirus 11p]. The December 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O39 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ckl|1ckl]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIV ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=343462 ADE1P]), CD46, MCP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2o39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o39 OCA], [https://pdbe.org/2o39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o39 RCSB], [https://www.ebi.ac.uk/pdbsum/2o39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o39 ProSAT]</span></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=2o39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o39 OCA], [https://pdbe.org/2o39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o39 RCSB], [https://www.ebi.ac.uk/pdbsum/2o39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o39 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/MCP_HUMAN MCP_HUMAN]] Defects in CD46 are a cause of susceptibility to hemolytic uremic syndrome atypical type 2 (AHUS2) [MIM:[https://omim.org/entry/612922 612922]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations.<ref>PMID:14615110</ref> <ref>PMID:14566051</ref> <ref>PMID:16621965</ref> <ref>PMID:16386793</ref> <ref>PMID:20513133</ref> 
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SPIKE_ADE1P SPIKE_ADE1P]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. [[https://www.uniprot.org/uniprot/MCP_HUMAN MCP_HUMAN]] Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. A number of viral and bacterial pathogens seem to exploit this property and directly induce an immunosuppressive phenotype in T-cells by binding to CD46.<ref>PMID:10843656</ref> <ref>PMID:12540904</ref> 
[https://www.uniprot.org/uniprot/SPIKE_ADE1P SPIKE_ADE1P] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ade1p]]
[[Category: Adenovirus]]
[[Category: Adenovirus]]
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Human adenovirus 11p]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Arnberg, N]]
[[Category: Arnberg N]]
[[Category: Persson, D B]]
[[Category: Persson DB]]
[[Category: Reiter, D M]]
[[Category: Reiter DM]]
[[Category: Stehle, T]]
[[Category: Stehle T]]
[[Category: Ad11]]
[[Category: Ccp]]
[[Category: Cd46]]
[[Category: Complement control protein]]
[[Category: Fiber knob]]
[[Category: Mcp]]
[[Category: Membrane cofactor protein]]
[[Category: Scr]]
[[Category: Short consensus repeat]]
[[Category: Viral protein-immune system complex]]
[[Category: Virus receptor complex]]

Revision as of 03:13, 28 December 2023

Human Adenovirus type 11 knob in complex with domains SCR1 and SCR2 of CD46 (membrane cofactor protein, MCP)Human Adenovirus type 11 knob in complex with domains SCR1 and SCR2 of CD46 (membrane cofactor protein, MCP)

Structural highlights

2o39 is a 4 chain structure with sequence from Homo sapiens and Human adenovirus 11p. The December 2010 RCSB PDB Molecule of the Month feature on Adenovirus by David Goodsell is 10.2210/rcsb_pdb/mom_2010_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPIKE_ADE1P Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Adenoviruses (Ads) are important human pathogens and valuable gene delivery vehicles. We report here the crystal structure of the species B Ad11 knob complexed with the Ad11-binding region of its receptor CD46. The conformation of bound CD46 differs profoundly from its unbound state, with the bent surface structure straightened into an elongated rod. This mechanism of interaction is likely to be conserved among many pathogens that target CD46 or related molecules.

Adenovirus type 11 binding alters the conformation of its receptor CD46.,Persson BD, Reiter DM, Marttila M, Mei YF, Casasnovas JM, Arnberg N, Stehle T Nat Struct Mol Biol. 2007 Feb;14(2):164-6. Epub 2007 Jan 14. PMID:17220899[1]

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

References

  1. ↑ Persson BD, Reiter DM, Marttila M, Mei YF, Casasnovas JM, Arnberg N, Stehle T. Adenovirus type 11 binding alters the conformation of its receptor CD46. Nat Struct Mol Biol. 2007 Feb;14(2):164-6. Epub 2007 Jan 14. PMID:17220899 doi:10.1038/nsmb1190

2o39, resolution 2.85Å

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