title   
  

Structural characterization of recombinant bovine Go alpha by spectroscopy and homology modeling

Tiber, Pınar and Orun, Oya and Nacar, Cevdet and Sezerman, Uğur and Severcan, Feride and Severcan, Mete and Matagne, André and Kan, Beki (2011) Structural characterization of recombinant bovine Go alpha by spectroscopy and homology modeling. Spectroscopy, 26 (4-5). pp. 213-229. ISSN 0712-4813

This is the latest version of this item.

[img]PDF - Registered users only - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
823Kb

Official URL: http://dx.doi.org/10.3233/SPE-2011-0543

Abstract

Go, a member of heterotrimeric guanine nucleotide-binding proteins, is the most abundant form of G protein in the central and peripheral nervous systems. Go alpha has a significant role in neuronal development and function but its signal transduction mechanism remains to be clarified. In this study, the bovine Go alpha subunit was overexpressed and purified into homogeneity. Its activity was studied using [(35)S] GTP gamma S binding, intrinsic fluorescence and BODIPY assays. The secondary structure was determined by both FTIR and CD spectroscopy as 42.3% alpha-helix, 13.4% beta-sheet and 24.3% beta-turn. A theoretical structure model was constructed. The structure from homology modeling is in very good agreement with the crystal structure of mouse Go alpha subunit except for the loop between alpha B-alpha C helices. This model was docked to the mouse RGS16 molecule. T117 on the alpha B-alpha C loop of Go alpha interacted with K172 on RGS16 as opposed to the T117 and K164 interaction in mouse.

Item Type:Article
Uncontrolled Keywords:Go alpha protein; FTIR spectroscopy; circular dichroism; homology modeling
Subjects:Q Science > Q Science (General)
ID Code:18961
Deposited By:Uğur Sezerman
Deposited On:05 Apr 2012 10:36
Last Modified:05 Apr 2012 10:36

Available Versions of this Item

Repository Staff Only: item control page