2n52

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'''Unreleased structure'''
 
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The entry 2n52 is ON HOLD
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==The solution structure of the kallikrein inhibitor SPINK6==
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<StructureSection load='2n52' size='340' side='right'caption='[[2n52]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N52 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">Solution NMR, 20 models</td></tr>
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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=2n52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n52 OCA], [https://pdbe.org/2n52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n52 RCSB], [https://www.ebi.ac.uk/pdbsum/2n52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n52 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ISK6_HUMAN ISK6_HUMAN] Serine protease inhibitor selective for kallikreins. Efficiently inhibits KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14. Doesn't inhibit KLK8.<ref>PMID:20667819</ref> <ref>PMID:21439340</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kallikrein-related peptidases (KLKs) are crucial for epidermal barrier function and are involved in the proteolytic regulation of the desquamation process. Elevated KLK levels were reported in atopic dermatitis. In skin, the proteolytic activity of KLKs is regulated by specific inhibitors of the serine protease inhibitor of Kazal-type (SPINK) family. SPINK6 was shown to be expressed in human stratum corneum and is able to inhibit several KLKs such as KLK4, -5, -12, -13 and -14. In order to understand the structural traits of the specific inhibition we solved the structure of SPINK6 in solution by NMR-spectroscopy and studied its interaction with KLKs. Thereby, beside the conserved binding mode, we identified an alternate binding mode which has so far not been observed for SPINK inhibitors.
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Authors: Grotzinger, J.
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The solution structure of the kallikrein-related peptidases inhibitor SPINK6.,Jung S, Fischer J, Spudy B, Kerkow T, Sonnichsen FD, Xue L, Bonvin AM, Goettig P, Magdolen V, Meyer-Hoffert U, Grotzinger J Biochem Biophys Res Commun. 2016 Feb 26;471(1):103-8. doi:, 10.1016/j.bbrc.2016.01.172. Epub 2016 Jan 30. PMID:26828269<ref>PMID:26828269</ref>
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Description: The solution structure of the kallikrein inhibitor SPINK6
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Grotzinger, J]]
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<div class="pdbe-citations 2n52" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Grotzinger J]]

Current revision

The solution structure of the kallikrein inhibitor SPINK6

PDB ID 2n52

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