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[[Image:1wav.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1wav", creates the "Structure Box" on the page.
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{{STRUCTURE_1wav|  PDB=1wav  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN'''


==CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN==
<StructureSection load='1wav' size='340' side='right'caption='[[1wav]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wav]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPH:PHENOL'>IPH</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'>[https://proteopedia.org/fgij/fg.htm?mol=1wav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wav OCA], [https://pdbe.org/1wav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wav RCSB], [https://www.ebi.ac.uk/pdbsum/1wav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wav ProSAT]</span></td></tr>
</table>
== Function ==
[https://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/wa/1wav_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1wav ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The form-B monoclinic insulin crystal was obtained from the sodium citrate buffer with 1% zinc chloride, keeping phenolic content between 0.76% and 1.25%. Its space group is P2(1), cell constants are: a = 4.924 nm, b = 6.094 nm, c = 4.818 nm, beta = 95.8 degrees. There are 6 insulin molecules which form a hexamer. The initial phase was obtained by using rotation function program of X-PLOR program package and molecular packing program of our laboratory. The molecular model was chosen from 4 zinc bovine insulin hexamer. After the preliminary refinement by using the macromolecular rigid body refinement technique, the molecular model was further refined and adjusted by using the energy-minimizing stereochemically restrained least-squared refinement on the difference Fourier maps. The final R-factor is 22.4% at 0.3 nm resolution, the r.m.s. deviations from standard bond length and bond angle are 0.0022 nm and 4.7 degrees, respectively.


==Overview==
Molecular replacement study on form-B monoclinic crystal of insulin.,Ding J, Wan Z, Chang W, Liang D Sci China C Life Sci. 1996 Apr;39(2):144-53. PMID:8760462<ref>PMID:8760462</ref>
The form-B monoclinic insulin crystal was obtained from the sodium citrate buffer with 1% zinc chloride, keeping phenolic content between 0.76% and 1.25%. Its space group is P2(1), cell constants are: a = 4.924 nm, b = 6.094 nm, c = 4.818 nm, beta = 95.8 degrees. There are 6 insulin molecules which form a hexamer. The initial phase was obtained by using rotation function program of X-PLOR program package and molecular packing program of our laboratory. The molecular model was chosen from 4 zinc bovine insulin hexamer. After the preliminary refinement by using the macromolecular rigid body refinement technique, the molecular model was further refined and adjusted by using the energy-minimizing stereochemically restrained least-squared refinement on the difference Fourier maps. The final R-factor is 22.4% at 0.3 nm resolution, the r.m.s. deviations from standard bond length and bond angle are 0.0022 nm and 4.7 degrees, respectively.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1WAV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAV OCA].
</div>
<div class="pdbe-citations 1wav" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Molecular replacement study on form-B monoclinic crystal of insulin., Ding J, Wan Z, Chang W, Liang D, Sci China C Life Sci. 1996 Apr;39(2):144-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8760462 8760462]
*[[Insulin 3D Structures|Insulin 3D Structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Chang, W R.]]
[[Category: Chang W-R]]
[[Category: Ding, J H.]]
[[Category: Ding J-H]]
[[Category: Liang, D C.]]
[[Category: Liang D-C]]
[[Category: Wan, Z L.]]
[[Category: Wan Z-L]]
[[Category: Hormone]]
[[Category: Insulin]]
[[Category: Phenol]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:23:56 2008''
Retrieved from "https://proteopedia.org/1wav"