1gcn
From Proteopedia
m (Protected "1gcn" [edit=sysop:move=sysop]) |
Revision as of 12:23, 28 December 2010
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| 1gcn, resolution 3.00Å () | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1gcn is a 1 chain structure of [[]] with sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
- Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T. X-ray analysis of glucagon and its relationship to receptor binding. Nature. 1975 Oct 30;257(5529):751-7. PMID:171582
