This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1b17

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:58, 8 November 2017

PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.00 COORDINATES)

Structural highlights

1b17 is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1b18, 1b19, 1b2a, 1b2b, 1b2c, 1b2d, 1b2e, 1b2f, 1b2g
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single conformation at pH </= 5.80, two conformations between pH 6.00 and 6.98 and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the conformation of GluB13 switches from one rotamer to another rotamer. Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational change. By pH 9.00 many residues have undergone relatively large shifts and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the observed and calculated structure factors and map correlation coefficients indicate that the porcine insulin structure changes gradually as a function of pH.

Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding.,Diao J Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):670-6. Epub 2003, Mar 25. PMID:12657786^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Diao J. Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding. Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):670-6. Epub 2003, Mar 25. PMID:12657786

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b17"

@@ Line 1: / Line 1: @@
 ==PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.00 COORDINATES)==
 <StructureSection load='1b17' size='340' side='right' caption='[[1b17]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b18|1b18]], [[1b19|1b19]], [[1b2a|1b2a]], [[1b2b|1b2b]], [[1b2c|1b2c]], [[1b2d|1b2d]], [[1b2e|1b2e]], [[1b2f|1b2f]], [[1b2g|1b2g]]</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=1b17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b17 OCA], [http://pdbe.org/1b17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b17 RCSB], [http://www.ebi.ac.uk/pdbsum/1b17 PDBsum]</span></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=1b17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b17 OCA], [http://pdbe.org/1b17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b17 RCSB], [http://www.ebi.ac.uk/pdbsum/1b17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b17 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1b17" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Molecular Playground/Insulin|Molecular Playground/Insulin]]
 == References ==
 <references/>

1b17

From Proteopedia

Revision as of 10:58, 8 November 2017

PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.00 COORDINATES)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox