5azz: Difference between revisions

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-'''Unreleased structure'''
-The entry 5azz is ON HOLD  until May 03 2018
+==Crystal structure of seleno-insulin==
+<StructureSection load='5azz' size='340' side='right' caption='[[5azz]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5azz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZZ FirstGlance]. <br>
+</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=5azz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azz OCA], [http://pdbe.org/5azz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azz RCSB], [http://www.ebi.ac.uk/pdbsum/5azz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN]] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Synthetic insulin analogues with a long lifetime are current drug targets for the therapy of diabetic patients. The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can enhance the lifetime of insulin in the presence of the insulin-degrading enzyme (IDE) without impairing the hormonal function. The [C7UA ,C7UB ] variant of bovine pancreatic insulin (BPIns) was successfully prepared by using two selenocysteine peptides (i.e., the C7U analogues of A- and B-chains, respectively). In a buffer solution at pH 10 they spontaneously assembled under thermodynamic control to the correct insulin fold. The selenoinsulin (Se-Ins) exhibited a bioactivity comparable to that of BPIns. Interestingly, degradation of Se-Ins with IDE was significantly decelerated (tau1/2 approximately 8 h vs. approximately 1 h for BPIns). The lifetime enhancement could be due to both the intrinsic stability of the diselenide bond and local conformational changes induced by the substitution.
-Authors: Watanabe, S., Okumura, M., Arai, K., Takei, T., Asahina, Y., Hojo, H., Iwaoka, M., Inaba, K.
+Preparation of Selenoinsulin as a Long-Lasting Insulin Analogue.,Arai K, Takei T, Okumura M, Watanabe S, Amagai Y, Asahina Y, Moroder L, Hojo H, Inaba K, Iwaoka M Angew Chem Int Ed Engl. 2017 May 8;56(20):5522-5526. doi: 10.1002/anie.201701654., Epub 2017 Apr 10. PMID:28394477<ref>PMID:28394477</ref>
-Description: Crystal structure of seleno-insulin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Inaba, K]]
+<div class="pdbe-citations 5azz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Arai, K]]
 [[Category: Asahina, Y]]
-[[Category: Watanabe, S]]
 [[Category: Hojo, H]]
-[[Category: Takei, T]]
+[[Category: Inaba, K]]
 [[Category: Iwaoka, M]]
 [[Category: Okumura, M]]
+[[Category: Takei, T]]
+[[Category: Watanabe, S]]
+[[Category: Hormone]]
+[[Category: Insulin]]
+[[Category: Selenocysteine]]