1xda
From Proteopedia
(New page: 200px<br /> <applet load="1xda" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xda, resolution 1.8Å" /> '''STRUCTURE OF INSULIN...) |
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| - | [[Image:1xda.gif|left|200px]]<br /> | + | [[Image:1xda.gif|left|200px]]<br /><applet load="1xda" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xda" size=" | + | |
caption="1xda, resolution 1.8Å" /> | caption="1xda, resolution 1.8Å" /> | ||
'''STRUCTURE OF INSULIN'''<br /> | '''STRUCTURE OF INSULIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human | + | The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human insulin, has been crystallized and the structure determined by X-ray crystallography. The fatty acid substituent on residue B29 Lys binds reversibly to circulating albumin protein in vivo, and by this mechanism the hormone's action is prolonged. Crystals of the fatty acid insulin grow in space group R3, with two dimers in the asymmetric unit, and diffract to 1.8 A spacing. The structure has been solved by molecular replacement and refined using a maximum likelihood method. The crystal structure consists of R6 zinc insulin hexamers which contain phenol. The fatty acids can be seen bound between the hexamers, making specific interactions with the side chains of residue B1 Phe; however, the lysine side chains to which the fatty acids are covalently attached are mostly disordered. The mode of binding of the fatty acids appears to be determined by crystal packing, and whether or not they interact with the protein in this way in solution remains uncertain. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XDA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CL, IPH and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XDA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=IPH:'>IPH</scene> and <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Havelund, S.]] | [[Category: Havelund, S.]] | ||
[[Category: Jonassen, I.]] | [[Category: Jonassen, I.]] | ||
| - | [[Category: Whittingham, J | + | [[Category: Whittingham, J L.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: IPH]] | [[Category: IPH]] | ||
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[[Category: metabolic role]] | [[Category: metabolic role]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:34 2008'' |
Revision as of 13:53, 21 February 2008
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STRUCTURE OF INSULIN
Contents |
Overview
The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human insulin, has been crystallized and the structure determined by X-ray crystallography. The fatty acid substituent on residue B29 Lys binds reversibly to circulating albumin protein in vivo, and by this mechanism the hormone's action is prolonged. Crystals of the fatty acid insulin grow in space group R3, with two dimers in the asymmetric unit, and diffract to 1.8 A spacing. The structure has been solved by molecular replacement and refined using a maximum likelihood method. The crystal structure consists of R6 zinc insulin hexamers which contain phenol. The fatty acids can be seen bound between the hexamers, making specific interactions with the side chains of residue B1 Phe; however, the lysine side chains to which the fatty acids are covalently attached are mostly disordered. The mode of binding of the fatty acids appears to be determined by crystal packing, and whether or not they interact with the protein in this way in solution remains uncertain.
Disease
Known diseases associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]
About this Structure
1XDA is a Protein complex structure of sequences from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a prolonged-acting insulin with albumin-binding properties., Whittingham JL, Havelund S, Jonassen I, Biochemistry. 1997 Mar 11;36(10):2826-31. PMID:9062110
Page seeded by OCA on Thu Feb 21 15:53:34 2008
Categories: Homo sapiens | Protein complex | Havelund, S. | Jonassen, I. | Whittingham, J L. | CL | IPH | MYR | ZN | Chemical activity | Diabetes | Fatty acid | Glucose metabolism | Hormone | Insulin albumin | Metabolic role
