4rpu
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal Structure of Human Presequence Protease in Complex with Inhibitor MitoBloCK-60== |
| - | + | <StructureSection load='4rpu' size='340' side='right' caption='[[4rpu]], [[Resolution|resolution]] 2.27Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4rpu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RPU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RPU FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3UE:[4-(DIPHENYLMETHYL)PIPERAZIN-1-YL](3-METHYL-4-NITROPHENYL)METHANONE'>3UE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</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=4rpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rpu OCA], [http://pdbe.org/4rpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rpu RCSB], [http://www.ebi.ac.uk/pdbsum/4rpu PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[Category: King, J | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/PREP_HUMAN PREP_HUMAN]] ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.<ref>PMID:16849325</ref> |
| - | [[Category: | + | == References == |
| - | [[Category: Mo, S | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: King, J V]] | ||
| + | [[Category: Koehler, C M]] | ||
| + | [[Category: Liang, W G]] | ||
| + | [[Category: Mo, S M]] | ||
| + | [[Category: Tang, W J]] | ||
[[Category: Wijaya, J]] | [[Category: Wijaya, J]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Revision as of 13:46, 9 December 2015
Crystal Structure of Human Presequence Protease in Complex with Inhibitor MitoBloCK-60
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