3e1x

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{{Seed}}
 
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[[Image:3e1x.jpg|left|200px]]
 
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==The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution==
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The line below this paragraph, containing "STRUCTURE_3e1x", creates the "Structure Box" on the page.
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<StructureSection load='3e1x' size='340' side='right'caption='[[3e1x]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e1x]] 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=3E1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1X FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3e1x| PDB=3e1x | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1x OCA], [https://pdbe.org/3e1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1x RCSB], [https://www.ebi.ac.uk/pdbsum/3e1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRSS8_HUMAN PRSS8_HUMAN] Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G).<ref>PMID:15246975</ref> <ref>PMID:15474520</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e1x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Prostasin or human channel-activating protease 1 has been reported to play a critical role in the regulation of extracellular sodium ion transport via its activation of the epithelial cell sodium channel. Here, the structure of the extracellular portion of the membrane associated serine protease has been solved to high resolution in complex with a nonselective d-FFR chloromethyl ketone inhibitor, in an apo form, in a form where the apo crystal has been soaked with the covalent inhibitor camostat and in complex with the protein inhibitor aprotinin. It was also crystallized in the presence of the divalent cation Ca(+2). Comparison of the structures with each other and with other members of the trypsin-like serine protease family reveals unique structural features of prostasin and a large degree of conformational variation within specificity determining loops. Of particular interest is the S1 subsite loop which opens and closes in response to basic residues or divalent ions, directly binding Ca(+2) cations. This induced fit active site provides a new possible mode of regulation of trypsin-like proteases adapted in particular to extracellular regions with variable ionic concentrations such as the outer membrane layer of the epithelial cell.
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===The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution===
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Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.,Spraggon G, Hornsby M, Shipway A, Tully DC, Bursulaya B, Danahay H, Harris JL, Lesley SA Protein Sci. 2009 May;18(5):1081-94. PMID:19388054<ref>PMID:19388054</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19388054}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3e1x" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19388054 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19388054}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3E1X is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1X OCA].
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==Reference==
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<ref group="xtra">PMID:19388054</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Harris, J L.]]
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[[Category: Large Structures]]
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[[Category: Hornsby, M.]]
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[[Category: Harris JL]]
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[[Category: Lesley, S A.]]
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[[Category: Hornsby M]]
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[[Category: Shipway, A.]]
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[[Category: Lesley SA]]
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[[Category: Spraggon, G.]]
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[[Category: Shipway A]]
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[[Category: Cell membrane]]
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[[Category: Spraggon G]]
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[[Category: Channel activating protease]]
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[[Category: Enac]]
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[[Category: Glycoprotein]]
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[[Category: Hcap-1]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Prostasin]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Serine protease]]
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[[Category: Transmembrane]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 10:28:49 2009''
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Current revision

The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution

PDB ID 3e1x

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