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3gyl

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Revision as of 07:16, 1 November 2017

Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion.

Structural highlights

3gyl is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3eon, 3e1x, 3fvf
Gene:	hCAP1, PRSS8 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2]

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

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tong Z, Illek B, Bhagwandin VJ, Verghese GM, Caughey GH. Prostasin, a membrane-anchored serine peptidase, regulates sodium currents in JME/CF15 cells, a cystic fibrosis airway epithelial cell line. Am J Physiol Lung Cell Mol Physiol. 2004 Nov;287(5):L928-35. Epub 2004 Jul 9. PMID:15246975 doi:http://dx.doi.org/10.1152/ajplung.00160.2004
↑ Shipway A, Danahay H, Williams JA, Tully DC, Backes BJ, Harris JL. Biochemical characterization of prostasin, a channel activating protease. Biochem Biophys Res Commun. 2004 Nov 12;324(2):953-63. PMID:15474520 doi:http://dx.doi.org/10.1016/j.bbrc.2004.09.123
↑ Spraggon G, Hornsby M, Shipway A, Tully DC, Bursulaya B, Danahay H, Harris JL, Lesley SA. Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Protein Sci. 2009 May;18(5):1081-94. PMID:19388054 doi:10.1002/pro.118

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gyl"

@@ Line 1: / Line 1: @@
 ==Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion.==
 <StructureSection load='3gyl' size='340' side='right' caption='[[3gyl]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eon|3eon]], [[3e1x|3e1x]], [[3fvf|3fvf]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hCAP1, PRSS8 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gyl OCA], [http://pdbe.org/3gyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gyl RCSB], [http://www.ebi.ac.uk/pdbsum/3gyl PDBsum]</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=3gyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gyl OCA], [http://pdbe.org/3gyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gyl RCSB], [http://www.ebi.ac.uk/pdbsum/3gyl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gyl ProSAT]</span></td></tr>
 </table>
 == Function ==

3gyl

From Proteopedia

Revision as of 07:16, 1 November 2017

Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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