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| | <StructureSection load='2oq5' size='340' side='right'caption='[[2oq5]], [[Resolution|resolution]] 1.61Å' scene=''> | | <StructureSection load='2oq5' size='340' side='right'caption='[[2oq5]], [[Resolution|resolution]] 1.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oq5]] 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=2OQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQ5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</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]] 1.61Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMPRSS11E, DESC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene></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=2oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oq5 OCA], [https://pdbe.org/2oq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oq5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oq5 ProSAT]</span></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=2oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oq5 OCA], [https://pdbe.org/2oq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oq5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oq5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TM11E_HUMAN TM11E_HUMAN]] Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (By similarity).
| + | [https://www.uniprot.org/uniprot/TM11E_HUMAN TM11E_HUMAN] Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2oq5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2oq5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transmembrane protease serine 2|Transmembrane protease serine 2]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Huber, R]] | + | [[Category: Huber R]] |
| - | [[Category: Jacob, U]] | + | [[Category: Jacob U]] |
| - | [[Category: Kyrieleis, O J.P]] | + | [[Category: Kyrieleis OJP]] |
| - | [[Category: Madison, E L]] | + | [[Category: Madison EL]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Trypsin-like serine protease]]
| + | |
| - | [[Category: Tumor marker]]
| + | |
| - | [[Category: Type ii trans-membrane serine proteinase]]
| + | |
| Structural highlights
Function
TM11E_HUMAN Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
DESC1 was identified using gene-expression analysis between squamous cell carcinoma of the head and neck and normal tissue. It belongs to the type II transmembrane multidomain serine proteinases (TTSPs), an expanding family of serine proteinases, whose members are differentially expressed in several tissues. The biological role of these proteins is currently under investigation, although in some cases their participation in specific functions has been reported. This is the case for enteropeptidase, hepsin, matriptase and corin. Some members, including DESC1, are associated with cell differentiation and have been described as tumor markers. TTSPs belong to the type II transmembrane proteins that display, in addition to a C-terminal trypsin-like serine proteinase domain, a differing set of stem domains, a transmembrane segment and a short N-terminal cytoplasmic region. Based on sequence analysis, the TTSP family is subdivided into four subfamilies: hepsin/transmembrane proteinase, serine (TMPRSS); matriptase; corin; and the human airway trypsin (HAT)/HAT-like/DESC subfamily. Members of the hepsin and matriptase subfamilies are known structurally and here we present the crystal structure of DESC1 as a first member of the HAT/HAT-like/DESC subfamily in complex with benzamidine. The proteinase domain of DESC1 exhibits a trypsin-like serine proteinase fold with a thrombin-like S1 pocket, a urokinase-type plasminogen activator-type S2 pocket, to accept small residues, and an open hydrophobic S3/S4 cavity to accept large hydrophobic residues. The deduced substrate specificity for DESC1 differs markedly from that of other structurally known TTSPs. Based on surface analysis, we propose a rigid domain association for the N-terminal SEA domain with the back site of the proteinase domain.
Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family.,Kyrieleis OJ, Huber R, Ong E, Oehler R, Hunter M, Madison EL, Jacob U FEBS J. 2007 Apr;274(8):2148-60. Epub 2007 Mar 27. PMID:17388811[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kyrieleis OJ, Huber R, Ong E, Oehler R, Hunter M, Madison EL, Jacob U. Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family. FEBS J. 2007 Apr;274(8):2148-60. Epub 2007 Mar 27. PMID:17388811 doi:10.1111/j.1742-4658.2007.05756.x
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