1t5q: Difference between revisions

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New page: left|200px<br /> <applet load="1t5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t5q" /> '''Solution Structure of GIP(1-30)amide in TFE...
 
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[[Image:1t5q.gif|left|200px]]<br />
[[Image:1t5q.gif|left|200px]]<br /><applet load="1t5q" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1t5q" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1t5q" />
caption="1t5q" />
'''Solution Structure of GIP(1-30)amide in TFE/Water'''<br />
'''Solution Structure of GIP(1-30)amide in TFE/Water'''<br />


==Overview==
==Overview==
Glucose-dependent insulinotropic polypeptide is an incretin hormone that, stimulates insulin secretion and reduces postprandial glycaemic, excursions. The glucose-dependent action of GIP on pancreatic beta-cells, has attracted attention towards its exploitation as a potential drug for, type 2 diabetes. Use of NMR or X-ray crystallography is vital to determine, the three-dimensional structure of the peptide. Therefore, to understand, the basic structural requirements for the biological activity of GIP, the, solution structure of the major biologically active fragment, GIP(1-30)amide, was investigated by proton NMR spectroscopy and molecular, modelling. The structure is characterised by a full length alpha-helical, conformation between residues F(6) and A(28). This structural information, could play an important role in the design of therapeutic agents based, upon GIP receptor agonists.
Glucose-dependent insulinotropic polypeptide is an incretin hormone that stimulates insulin secretion and reduces postprandial glycaemic excursions. The glucose-dependent action of GIP on pancreatic beta-cells has attracted attention towards its exploitation as a potential drug for type 2 diabetes. Use of NMR or X-ray crystallography is vital to determine the three-dimensional structure of the peptide. Therefore, to understand the basic structural requirements for the biological activity of GIP, the solution structure of the major biologically active fragment, GIP(1-30)amide, was investigated by proton NMR spectroscopy and molecular modelling. The structure is characterised by a full length alpha-helical conformation between residues F(6) and A(28). This structural information could play an important role in the design of therapeutic agents based upon GIP receptor agonists.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1T5Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T5Q OCA].  
1T5Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5Q OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alana, I.]]
[[Category: Alana, I.]]
[[Category: Gault, V.A.]]
[[Category: Gault, V A.]]
[[Category: Harte, F.P.M.O.]]
[[Category: Harte, F P.M O.]]
[[Category: Hewage, C.M.]]
[[Category: Hewage, C M.]]
[[Category: Malthouse, J.P.G.]]
[[Category: Malthouse, J P.G.]]
[[Category: Parker, J.C.]]
[[Category: Parker, J C.]]
[[Category: diabetes]]
[[Category: diabetes]]
[[Category: gip]]
[[Category: gip]]
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[[Category: obesity]]
[[Category: obesity]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:20:54 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:10 2008''