6czs: Difference between revisions
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==Crystal structure of human pro-cathepsin H C26S mutant== | |||
<StructureSection load='6czs' size='340' side='right' caption='[[6czs]], [[Resolution|resolution]] 1.66Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6czs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CZS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_H Cathepsin H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.16 3.4.22.16] </span></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=6czs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6czs OCA], [http://pdbe.org/6czs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6czs RCSB], [http://www.ebi.ac.uk/pdbsum/6czs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6czs ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN]] Narcolepsy-cataplexy. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN]] Important for the overall degradation of proteins in lysosomes. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases. It is the only known aminopeptidase in the family and is reported to be involved in cancer and other major diseases. Like many other proteases, it is synthesized as an inactive proenzyme. Although the crystal structure of mature porcine cathepsin H revealed the binding of the mini-chain and provided structural basis for the aminopeptidase activity, detailed structural and functional information on the inhibition and activation of procathepsin H has been elusive. Here we present the crystal structures of human procathepsin H at 2.00 A and 1.66 A resolution. These structures allow us to explore in detail the molecular basis for the inhibition of the mature domain by the prodomain. Comparison with cathepsin H structure reveals how mini-chain reorients upon activation. We further demonstrate that procathepsin H is not auto-activated but can be trans-activated by cathepsin L. | |||
Crystal structures of human procathepsin H.,Hao Y, Purtha W, Cortesio C, Rui H, Gu Y, Chen H, Sickmier EA, Manzanillo P, Huang X PLoS One. 2018 Jul 25;13(7):e0200374. doi: 10.1371/journal.pone.0200374., eCollection 2018. PMID:30044821<ref>PMID:30044821</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6czs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cathepsin H]] | |||
[[Category: Hao, Y]] | |||
[[Category: Huang, X]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inhibitory prodomain]] | |||
[[Category: Papain family cysteine peptidase]] | |||
[[Category: Protein degradation in lysosome]] | |||
