7ins

From Proteopedia

(Difference between revisions)

Revision as of 20:34, 25 December 2014

STRUCTURE OF PORCINE INSULIN COCRYSTALLIZED WITH CLUPEINE Z

Structural highlights

7ins is a 7 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:	, ,
Resources:	FirstGlance, OCA, RCSB, PDBsum

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

The crystal structure of NPH-insulin, pig insulin cocrystallized with zinc, m-cresol and protamine, has been solved by molecular replacement and refined using restrained least-squares refinement methods. The final crystallographic R factor for all reflections between 2 and 10 A is 19.4%. The insulin molecules are arranged as hexamers with two tetrahedrally coordinated Zn atoms in the central channel and one m-cresol bound to each monomer near His B5. One protamine binding site has been unequivocally identified near a dimer-dimer interface, although most of the polypeptide is crystallographically disordered. The conformation of the insulin moiety and the structural differences between the three unique monomers have been analysed. The zinc and m-cresol environments are described and the nature of the protamine binding site is outlined.

Structure of porcine insulin cocrystallized with clupeine Z.,Balschmidt P, Hansen FB, Dodson EJ, Dodson GG, Korber F Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):975-86. PMID:1772633^[1]

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

References

↑ Balschmidt P, Hansen FB, Dodson EJ, Dodson GG, Korber F. Structure of porcine insulin cocrystallized with clupeine Z. Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):975-86. PMID:1772633

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7ins"

@@ Line 6: / Line 6: @@
 <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=7ins FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ins OCA], [http://www.rcsb.org/pdb/explore.do?structureId=7ins RCSB], [http://www.ebi.ac.uk/pdbsum/7ins 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]]

7ins

From Proteopedia

Revision as of 20:34, 25 December 2014

STRUCTURE OF PORCINE INSULIN COCRYSTALLIZED WITH CLUPEINE Z

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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