User:Mary Ball/Glucagon
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Revision as of 12:53, 12 June 2010
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| 1gcn, resolution 3.00Å () | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Contents |
GLUCAGON
About this Structure
1GCN is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
For information on the function of gulcagon, see the Glucagon article in Wikipedia at [1].
X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING
X-ray analysis of the pancreatic hormone glucagon shows that in crystals the polypeptide adopts a mainly helical conformation, which is stabilised by hydrophobic interactions between molecules related by threefold symmetry. A model is presented in which the glucagon molecule exists in dilute solutions as an equilibrium population of conformers with little retention of conformers with little retention of structure, and in which the helical conformation is stablised by hydrophobic interactions either as an oligomer or as a complex with the receptor.
X-ray analysis of glucagon and its relationship to receptor binding., Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T, Nature. 1975 Oct 30;257(5529):751-7. PMID:171582
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Reference
X-ray analysis of glucagon and its relationship to receptor binding., Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T, Nature. 1975 Oct 30;257(5529):751-7. PMID:171582
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