6duj
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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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