5ei0: Difference between revisions
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==Structure of RCL-cleaved vaspin (serpinA12)== | ==Structure of RCL-cleaved vaspin (serpinA12)== | ||
<StructureSection load='5ei0' size='340' side='right' caption='[[5ei0]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5ei0' size='340' side='right'caption='[[5ei0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ei0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EI0 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5ei0]] is a 2 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=5EI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EI0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=5ei0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ei0 OCA], [https://pdbe.org/5ei0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ei0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ei0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ei0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SPA12_HUMAN SPA12_HUMAN] May modulate insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ei0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ei0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Serpin 3D structures|Serpin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Daberger J]] | ||
[[Category: Heiker JT]] | |||
[[Category: | [[Category: Kuettner BE]] | ||
[[Category: | [[Category: Pippel J]] | ||
[[Category: | [[Category: Schultz S]] | ||
[[Category: | [[Category: Strater N]] | ||
[[Category: | [[Category: Ulbricht D]] | ||
[[Category: | |||
Latest revision as of 09:28, 5 July 2023
Structure of RCL-cleaved vaspin (serpinA12)Structure of RCL-cleaved vaspin (serpinA12)
Structural highlights
FunctionSPA12_HUMAN May modulate insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. Publication Abstract from PubMedThe adipokine vaspin (serpinA12) is mainly expressed in white adipose tissue and exhibits various beneficial effects on obesity-related processes. Kallikrein 7 is the only known target protease of vaspin and is inhibited by the classical serpin inhibitory mechanism involving a cleavage of the reactive center loop between P1 (M378) and P1' (E379). Here, we present the x-ray structure of vaspin, cleaved between M378-E379. We provide a comprehensive analysis of differences between the uncleaved and cleaved forms in the shutter, breach, and hinge regions as well as helix F with relation to common molecular features underlying the serpin inhibitory mode. Furthermore, we point out differences towards other serpins and provide novel data underlining the remarkable stability of vaspin. We speculate that the previously reported FKGx1Wx2x3 motif in the breach region may play a decisive role in determining the reactive center loop configuration in the native vaspin state and might contribute to the high thermostability of vaspin. Thus, this structure may provide a basis for future mutational studies. Crystal structure of cleaved vaspin (serpinA12).,Pippel J, Kuettner EB, Ulbricht D, Daberger J, Schultz S, Heiker JT, Strater N Biol Chem. 2015 Nov 3. pii:, /j/bchm.just-accepted/hsz-2015-0229/hsz-2015-0229.xml. doi:, 10.1515/hsz-2015-0229. PMID:26529565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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