2l71

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[[Image:2l71.png|left|200px]]
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==NMR solution structure of GIP in Bicellular media==
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<StructureSection load='2l71' size='340' side='right' caption='[[2l71]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
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== Structural highlights ==
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[[2l71]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L71 OCA]. <br>
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<b>Related:</b> [[1t5q|1t5q]], [[2b4n|2b4n]], [[2obu|2obu]], [[2l70|2l70]]<br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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Glucose-dependent insulinotropic polypeptide (GIP) is an insulinotropic incretin hormone that stimulates insulin secretion during a meal. GIP has glucose lowering abilities and hence is considered as a potential target molecule for type 2 diabetes therapy. In this article, we present the solution structure of GIP in membrane-mimicking environments by proton NMR spectroscopy and molecular modelling. GIP adopts an alpha-helical conformation between residues Phe(6)-Gly(31) and Ala(13)-Gln(29) for micellar and bicellar media, respectively. Previously we examined the effect of N-terminal Ala substitution in GIP, but here eight GIP analogues were synthesised by replacing individual residues within the central 8-18 region with alanine. These studies showed relatively minor changes in biological activity as assessed by insulin releasing potency. However, at higher concentration, GIP(Ala(16)), and GIP(Ala(18)) showed insulin secreting activity higher than the native GIP (P&lt;0.01 to P&lt;0.001) in cultured pancreatic BRIN-BD11 cells. Receptor interaction studies of the native GIP with the extracellular domain of its receptor were performed by using two different docking algorithms. At the optimised docking conformation, the complex was stabilised by the presence of hydrophobic interactions and intermolecular hydrogen bonding. Further, we have identified some potentially important additional C-terminal interactions of GIP with its N-terminal extracellular receptor domain.
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Conformational, receptor interaction and alanine scan studies of glucose-dependent insulinotropic polypeptide.,Venneti KC, Malthouse JP, O'Harte FP, Hewage CM Biochim Biophys Acta. 2011 Jul;1814(7):882-8. Epub 2011 Apr 27. PMID:21539943<ref>PMID:21539943</ref>
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The line below this paragraph, containing "STRUCTURE_2l71", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2l71| PDB=2l71 | SCENE= }}
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===NMR solution structure of GIP in Bicellular media===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21539943}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 21539943 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21539943}}
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==About this Structure==
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[[2l71]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L71 OCA].
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==Reference==
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<ref group="xtra">PMID:021539943</ref><references group="xtra"/>
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[[Category: Alana, I.]]
[[Category: Alana, I.]]
[[Category: Harte, F P.M O.]]
[[Category: Harte, F P.M O.]]

Revision as of 08:34, 30 April 2014

NMR solution structure of GIP in Bicellular media

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