View source for 3ins

==STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT==
<StructureSection load='3ins' size='340' side='right' caption='[[3ins]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ins]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3INS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3INS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3ins FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ins OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ins RCSB], [http://www.ebi.ac.uk/pdbsum/3ins PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/INS_PIG INS_PIG]] 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. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/3ins_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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== Publication Abstract from PubMed ==
Neutron diffraction data for porcine 2Zn insulin were collected to 2.2 A resolution from a single crystal deuterated by slow exchange of mother liquor. A joint neutron/X-ray restrained-least-squares refinement was undertaken using the neutron data, as well as the 1.5 A resolution X-ray data collected previously. The final R factors were 0.182 for the X-ray data and 0.191 for the neutron data. Resulting atomic coordinates were compared with the initial X-ray model, showing a total r.m.s. shift of 0.36 A for the protein and 0.6 A for the solvent. Protonation of a number of individual amino acids was investigated by analysis of the neutron maps. No D atoms were found between the carboxylates of Glu B13 which make an intermolecular contact, suggesting nonbonded interaction rather than the predicted hydrogen bond. Amide hydrogen exchange was investigated in a refinement of their atomic occupancies. Regions of unexchanged amide groups were found in the center of the B helices. The results of this study emphasize the limited amount of information available in neutron diffraction studies of proteins at resolution lower than 2 A.

Structure of insulin: results of joint neutron and X-ray refinement.,Wlodawer A, Savage H, Dodson G Acta Crystallogr B. 1989 Feb 1;45 ( Pt 1):99-107. PMID:2695122<ref>PMID:2695122</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Molecular Playground/Insulin|Molecular Playground/Insulin]]
== References ==
<references/>
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</StructureSection>
[[Category: Pig]]
[[Category: Savage, H]]
[[Category: Wlodawer, A]]
[[Category: Hormone]]