کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10802965 | 1055760 | 2008 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural model of a complex between the heterotrimeric G protein, Gsα, and tubulin
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کلمات کلیدی
GTPaseGsαGtαSPR - تشدید پلاسمون سطحیSurface plasmon resonance - تشدید پلاسمون سطحیG protein - جی پروتئینMicrotubule - ریزلوله یا میکروتوبولCrystal structure - ساختار کریستالیMaps - نقشه هاmicrotubule-associated proteins - پروتئین های مرتبط با میکروتوبولCytoskeleton - چارچوب یاخته، سیتواسکلتون، اسکلت سلولیGiα - گیا
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural model of a complex between the heterotrimeric G protein, Gsα, and tubulin Structural model of a complex between the heterotrimeric G protein, Gsα, and tubulin](/preview/png/10802965.png)
چکیده انگلیسی
A number of studies have demonstrated interplay between the cytoskeleton and G protein signaling. Many of these studies have determined a specific interaction between tubulin, the building block of microtubules, and G proteins. The α subunits of some heterotrimeric G proteins, including Gsα, have been shown to interact strongly with tubulin. Binding of Gα to tubulin results in increased dynamicity of microtubules due to activation of GTPase of tubulin. Tubulin also activates Gsα via a direct transfer of GTP between these molecules. Structural insight into the interaction between tubulin and Gsα was required, and was determined, in this report, through biochemical and molecular docking techniques. Solid phase peptide arrays suggested that a portion of the amino terminus, α2-β4 (the region between switch II and switch III) and α3-β5 (just distal to the switch III region) domains of Gsα are important for interaction with tubulin. Molecular docking studies revealed the best-fit models based on the biochemical data, showing an interface between the two molecules that includes the adenylyl cyclase/Gβγ interaction regions of Gsα and the exchangeable nucleotide-binding site of tubulin. These structural models explain the ability of tubulin to facilitate GTP exchange on Gα and the ability of Gα to activate tubulin GTPase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 6, June 2008, Pages 964-973
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 6, June 2008, Pages 964-973
نویسندگان
Brian T. Layden, Witchuda Saengsawang, Robert J. Donati, Shuo Yang, Debbie C. Mulhearn, Michael E. Johnson, Mark M. Rasenick,