3hs0

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<StructureSection load='3hs0' size='340' side='right'caption='[[3hs0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3hs0' size='340' side='right'caption='[[3hs0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3hs0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Naja_kaouthia Naja kaouthia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HS0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3hs0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Naja_kaouthia Naja kaouthia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HS0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hrz|3hrz]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CFB, BF, BFD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alternative-complement-pathway_C3/C5_convertase Alternative-complement-pathway C3/C5 convertase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.47 3.4.21.47] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hs0 OCA], [https://pdbe.org/3hs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hs0 RCSB], [https://www.ebi.ac.uk/pdbsum/3hs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hs0 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=3hs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hs0 OCA], [https://pdbe.org/3hs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hs0 RCSB], [https://www.ebi.ac.uk/pdbsum/3hs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hs0 ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN]] Defects in CFB are a cause of susceptibility to hemolytic uremic syndrome atypical type 4 (AHUS4) [MIM:[https://omim.org/entry/612924 612924]]. 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.<ref>PMID:17182750</ref> <ref>PMID:20513133</ref>
 
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN]] Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. [[https://www.uniprot.org/uniprot/CO3_NAJKA CO3_NAJKA]] Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.
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[https://www.uniprot.org/uniprot/VCO3_NAJKA VCO3_NAJKA] Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.
== 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>
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[[Category: Alternative-complement-pathway C3/C5 convertase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Naja kaouthia]]
[[Category: Naja kaouthia]]
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[[Category: Fritzinger, D C]]
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[[Category: Fritzinger DC]]
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[[Category: Gomes, L]]
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[[Category: Gomes L]]
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[[Category: Gros, P]]
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[[Category: Gros P]]
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[[Category: Janssen, B J.C]]
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[[Category: Janssen BJC]]
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[[Category: Koning, R I]]
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[[Category: Koning RI]]
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[[Category: Koster, A J]]
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[[Category: Koster AJ]]
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[[Category: Svergun, D I]]
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[[Category: Svergun DI]]
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[[Category: Vogel, C W]]
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[[Category: Vogel C-W]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Complement alternate pathway]]
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[[Category: Complement pathway]]
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[[Category: Complement system]]
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[[Category: Convertase]]
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[[Category: Disulfide bond]]
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[[Category: Glycation]]
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[[Category: Glycoprotein]]
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[[Category: Glycosilated]]
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[[Category: Hydrolase]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Inflammatory response]]
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[[Category: Innate immunity]]
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[[Category: Multi-domain]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Serine protease]]
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[[Category: Sushi]]
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[[Category: Thioester bond]]
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[[Category: Zymogen]]
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Revision as of 07:27, 6 September 2023

Cobra Venom Factor (CVF) in complex with human factor B

PDB ID 3hs0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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