2kxk: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[2kxk]] is a 2 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=2KXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXK FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxk OCA], [https://pdbe.org/2kxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxk RCSB], [https://www.ebi.ac.uk/pdbsum/2kxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxk ProSAT]</span></td></tr>
+</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxk OCA], [https://pdbe.org/2kxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxk RCSB], [https://www.ebi.ac.uk/pdbsum/2kxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxk ProSAT]</span></td></tr>
 </table>
 == Disease ==
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 == Function ==
 [https://www.uniprot.org/uniprot/INS_HUMAN INS_HUMAN] 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 ==
-A tertiary structure of recombinant A22(G)-B31(K)-B32(R)-human insulin monomer (insulin GKR) has been characterized by (1)H, (13)C NMR at natural isotopic abundance using NOESY, TOCSY, (1)H/(13)C-GHSQC, and (1)H/(13)C-GHSQC-TOCSY spectra. Translational diffusion studies indicate the monomer structure in water/acetonitrile (65/35vol.%). CSI analysis confirms existence of secondary structure motifs present in human insulin standard (HIS). Both techniques allow to establish that in this solvent recombinant insulin GKR exists as a monomer. Starting from structures calculated by the program CYANA, two different refinement protocols used molecular dynamics simulated annealing with the program AMBER; in vacuum (AMBER_VC), and including a generalized Born solvent model (AMBER_GB). From these calculations an ensemble of 20 structures of lowest energy was chosen which represents the tertiary structure of studied insulin. Here we present novel insulin with added A22(G) amino acid which interacts with beta-turn environment resulting in high flexibility of B chain C-terminus.
-Novel recombinant insulin analogue with flexible C-terminus in B chain. NMR structure of biosynthetic engineered A22G-B31K-B32R human insulin monomer in water/acetonitrile solution.,Borowicz P, Bocian W, Sitkowski J, Bednarek E, Mikiewicz-Sygula D, Blazej-Sosnowska S, Bogiel M, Rusek D, Kurzynoga D, Kozerski L Int J Biol Macromol. 2011 Nov 1;49(4):548-54. Epub 2011 Jun 16. PMID:21704065<ref>PMID:21704065</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2kxk" style="background-color:#fffaf0;"></div>
 ==See Also==