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1aph

From Proteopedia

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(New page: 200px<br /><applet load="1aph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aph, resolution 2.0&Aring;" /> '''CONFORMATIONAL CHANGE...)
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[[Image:1aph.gif|left|200px]]<br /><applet load="1aph" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1aph, resolution 2.0&Aring;" />
 
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'''CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-11'''<br />
 
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==Overview==
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==CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-11==
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To determine the effect of variations in the charge distribution on the, conformation of a protein molecule, we have solved the structures of, bovine cubic insulin over a pH range from 7 to 11 in 0.1 M and 1 M sodium, salt solutions. The x-ray data were collected beyond 2-A resolution and, the R factors for the refined models ranged from 0.16 to 0.20. Whereas the, positions of most protein and well-ordered solvent atoms are conserved, about 30% of residues alter their predominant conformation as the pH is, changed. Conformational switching of A5 Gln and B10 His correlates with, the pH dependence of monovalent cation binding to insulin in cubic, crystals. Shifts in the relative positions of the A chain NH2-terminal and, B chain COOH-terminal groups are probably due to titration of the A1, alpha-amino group. Two alternative positions of B25 Phe and A21 Asn, observed in cubic insulin at pH 11 are similar to those found in two, independent molecules of the 2Zn insulin dimer at pH 6.4. The, conformational changes of the insulin amino acids appear to be only, loosely coupled at distant protein sites. Shifts in the equilibrium, between distinct conformational substates as the charge distribution on, the protein is altered are analogous to the electrostatically triggered, movements that occur in many functional protein reactions.
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<StructureSection load='1aph' size='340' side='right'caption='[[1aph]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1aph]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APH FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCE:1,2-DICHLOROETHANE'>DCE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aph OCA], [https://pdbe.org/1aph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aph RCSB], [https://www.ebi.ac.uk/pdbsum/1aph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aph ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1aph_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1aph ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1APH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with DCE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APH OCA].
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*[[Insulin 3D Structures|Insulin 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Conformational changes in cubic insulin crystals in the pH range 7-11., Gursky O, Badger J, Li Y, Caspar DL, Biophys J. 1992 Nov;63(5):1210-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1477273 1477273]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Badger, J.]]
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[[Category: Badger J]]
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[[Category: Caspar, D.L.D.]]
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[[Category: Caspar DLD]]
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[[Category: Gursky, O.]]
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[[Category: Gursky O]]
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[[Category: Li, Y.]]
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[[Category: Li Y]]
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[[Category: DCE]]
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[[Category: hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:01:30 2007''
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Current revision

CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS IN THE PH RANGE 7-11

PDB ID 1aph

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