1gcn
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(New page: 200px<br /><applet load="1gcn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcn, resolution 3.0Å" /> '''X-RAY ANALYSIS OF GLU...)
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Revision as of 13:49, 20 November 2007
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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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