1gcn
From Proteopedia
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{{STRUCTURE_1gcn| PDB=1gcn | SCENE= }} | {{STRUCTURE_1gcn| PDB=1gcn | SCENE= }} | ||
| - | + | ===X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING=== | |
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| - | + | The line below this paragraph, {{ABSTRACT_PUBMED_171582}}, adds the Publication Abstract to the page | |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 171582 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_171582}} | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Tickle, I J.]] | [[Category: Tickle, I J.]] | ||
[[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 Tue Jul 1 05:05:13 2008'' | ||
Revision as of 02:05, 1 July 2008
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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 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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