2zv6: Difference between revisions
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==Crystal structure of human squamous cell carcinoma antigen 1== | ==Crystal structure of human squamous cell carcinoma antigen 1== | ||
<StructureSection load='2zv6' size='340' side='right' caption='[[2zv6]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2zv6' size='340' side='right'caption='[[2zv6]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zv6]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2zv6]] is a 3 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=2ZV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZV6 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINB3, SCCA, SCCA1 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINB3, SCCA, SCCA1 ([https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zv6 OCA], [https://pdbe.org/2zv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zv6 RCSB], [https://www.ebi.ac.uk/pdbsum/2zv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zv6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SPB3_HUMAN SPB3_HUMAN]] May act as a protease inhibitor to modulate the host immune response against tumor cells. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Serpin|Serpin]] | *[[Serpin 3D structures|Serpin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Hibino, T]] | [[Category: Hibino, T]] | ||
[[Category: Katagiri, C]] | [[Category: Katagiri, C]] | ||
Revision as of 20:38, 15 December 2021
Crystal structure of human squamous cell carcinoma antigen 1Crystal structure of human squamous cell carcinoma antigen 1
Structural highlights
Function[SPB3_HUMAN] May act as a protease inhibitor to modulate the host immune response against tumor cells. 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 PubMedSquamous cell carcinoma antigen 1 (SCCA1), which belongs to serine proteinase inhibitor (serpin) superfamily, inhibits papain-like cysteine proteinase. Recently, it has been reported that SCCA1 acts not only as a proteinase inhibitor but also as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1). The present study determined the crystal structure of SCCA1, suggesting that the reactive center loop (RCL) of SCCA1, a recognition site of proteinase, is very flexible and located away form the main-body of SCCA1. We show that the inhibitory effect of SCCA1 on the kinase activity of JNK1 is lost when the RCL was truncated. Furthermore, we found that a mutant protein created by replacing one amino acid in RCL maintain the suppressive activity to JNK1, whereas the inhibitory effect to proteinase is obviously decreased. Crystal structure of SCCA1 and insight about the interaction with JNK1.,Zheng B, Matoba Y, Kumagai T, Katagiri C, Hibino T, Sugiyama M Biochem Biophys Res Commun. 2009 Feb 27;380(1):143-7. Epub 2009 Jan 21. PMID:19166818[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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