1gcn
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcn OCA], [http://www.ebi.ac.uk/pdbsum/1gcn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gcn RCSB]</span> | ||
}} | }} | ||
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[[Category: hormone]] | [[Category: hormone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:29 2008'' |
Revision as of 17:41, 30 March 2008
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| , resolution 3.0Å | |||||||
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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
Overview
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.
About this Structure
1GCN is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
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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