6duj: Difference between revisions
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==Crystal structure of A51V variant of Human Cytochrome c== | |||
<StructureSection load='6duj' size='340' side='right'caption='[[6duj]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6duj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DUJ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | |||
[[Category: | <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=6duj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6duj OCA], [http://pdbe.org/6duj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6duj RCSB], [http://www.ebi.ac.uk/pdbsum/6duj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6duj ProSAT]</span></td></tr> | ||
[[Category: Bowler, B | </table> | ||
== Disease == | |||
[[http://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Defects in CYCS are the cause of thrombocytopenia type 4 (THC4) [MIM:[http://omim.org/entry/612004 612004]]; also known as autosomal dominant thrombocytopenia type 4. Thrombocytopenia is the presence of relatively few platelets in blood. THC4 is a non-syndromic form of thrombocytopenia. Clinical manifestations of thrombocytopenia are absent or mild. THC4 may be caused by dysregulated platelet formation.<ref>PMID:18345000</ref> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CYC_HUMAN CYC_HUMAN]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Bowler, B E]] | |||
[[Category: Lei, H]] | [[Category: Lei, H]] | ||
[[Category: Apoptosis]] | |||
[[Category: Heme]] | |||
[[Category: Peroxidase activity]] | |||
Revision as of 06:44, 26 June 2019
Crystal structure of A51V variant of Human Cytochrome c
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