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| | <StructureSection load='6czk' size='340' side='right'caption='[[6czk]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6czk' size='340' side='right'caption='[[6czk]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6czk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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://proteopedia.org/fgij/fg.htm?mol=6CZK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6czk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6CZK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSH, CPSB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6czk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6czk OCA], [https://pdbe.org/6czk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6czk RCSB], [https://www.ebi.ac.uk/pdbsum/6czk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6czk ProSAT]</span></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://proteopedia.org/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> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN]] Narcolepsy-cataplexy. | + | [https://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN] Narcolepsy-cataplexy. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN]] Important for the overall degradation of proteins in lysosomes. | + | [https://www.uniprot.org/uniprot/CATH_HUMAN CATH_HUMAN] Important for the overall degradation of proteins in lysosomes. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cathepsin H]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hao, Y]] | + | [[Category: Hao Y]] |
| - | [[Category: Huang, X]] | + | [[Category: Huang X]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitory prodomain]]
| + | |
| - | [[Category: Papain family cysteine peptidase]]
| + | |
| - | [[Category: Protein degradation in lysosome]]
| + | |
| Structural highlights
6czk is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.001Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
CATH_HUMAN Narcolepsy-cataplexy.
Function
CATH_HUMAN Important for the overall degradation of proteins in lysosomes.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hao Y, Purtha W, Cortesio C, Rui H, Gu Y, Chen H, Sickmier EA, Manzanillo P, Huang X. Crystal structures of human procathepsin H. PLoS One. 2018 Jul 25;13(7):e0200374. doi: 10.1371/journal.pone.0200374., eCollection 2018. PMID:30044821 doi:http://dx.doi.org/10.1371/journal.pone.0200374
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