6czk: Difference between revisions
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==Crystal structure of wild-type human pro-cathepsin H== | |||
<StructureSection load='6czk' size='340' side='right' caption='[[6czk]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6czk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CZK 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=GOL:GLYCEROL'>GOL</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></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</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=6czk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6czk OCA], [http://pdbe.org/6czk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6czk RCSB], [http://www.ebi.ac.uk/pdbsum/6czk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6czk 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 6czk" 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]] | |||
Revision as of 00:47, 10 August 2018
Crystal structure of wild-type human pro-cathepsin HCrystal structure of wild-type human pro-cathepsin H
Structural highlights
Disease[CATH_HUMAN] Narcolepsy-cataplexy. Function[CATH_HUMAN] Important for the overall degradation of proteins in lysosomes. Publication Abstract from PubMedCathepsin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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