1gcn

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[[Image:1gcn.gif|left|200px]]
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{{Structure
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|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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'''X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING'''
'''X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING'''
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[[Category: Sasaki, K.]]
[[Category: Sasaki, K.]]
[[Category: Tickle, I J.]]
[[Category: Tickle, I J.]]
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[[Category: hormone]]
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[[Category: Hormone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:25:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:29 2008''
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Revision as of 14:25, 2 May 2008

Image:1gcn.gif


PDB ID 1gcn

Drag the structure with the mouse to rotate
1gcn, resolution 3.00Å ()
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 Page seeded by OCA on Fri May 2 17:25:06 2008

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