6ins

From Proteopedia

(Difference between revisions)

Revision as of 14:09, 25 December 2014

X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE

Structural highlights

6ins 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:
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

A crystal structure of a totally inactive insulin molecule has been determined. For this insulin molecule, the first without detectable activity to be characterized, the A and B-chains are linked by a peptide bond between A1 Gly and B29 Lys. The molecule has retained all its normal self-association properties and it can also accommodate the two different conformations designated T and R, as seen in 4Zn native pig insulin crystals. The hexamers of the crosslinked insulin molecule were crystallized using the 4Zn insulin recipe of Schlichtkrull. The structure has been crystallographically refined with data extending to 2 A using restrained least-square methods. Comparison of the B29-A1 peptide crosslink insulin and the 4Zn native insulin reveals close structural similarities with the native dimer. The analysis of the structure confirms the earlier hypothesis that insulin structures in crystals are not in an active conformation and that a separation of N-terminal A-chain and C-terminal B-chain is required for interaction with the insulin receptor.

X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue.,Derewenda U, Derewenda Z, Dodson EJ, Dodson GG, Bing X, Markussen J J Mol Biol. 1991 Jul 20;220(2):425-33. PMID:1856866^[1]

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

References

↑ Derewenda U, Derewenda Z, Dodson EJ, Dodson GG, Bing X, Markussen J. X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue. J Mol Biol. 1991 Jul 20;220(2):425-33. PMID:1856866

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/6ins"

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

6ins

From Proteopedia

Revision as of 14:09, 25 December 2014

X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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