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Structural and Functional Studies of...

Watanabe, Akira.

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Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus./
作者:	Watanabe, Akira.
面頁冊數:	129 p.
附註:	Source: Dissertation Abstracts International, Volume: 74-03(E), Section: B.
Contained By:	Dissertation Abstracts International74-03B(E).
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3532488
ISBN:	9781267753984

Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus.
Watanabe, Akira.

Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus. - 129 p.

Source: Dissertation Abstracts International, Volume: 74-03(E), Section: B.

Thesis (Ph.D.)--University of California, Los Angeles, 2012.

Secondary active transporters are essential components of physiology in all organisms. They utilize the energy stored in electrochemical gradients of ions to pump specific molecules across the otherwise impermeable membrane bilayer that surrounds all cells and organelles. They are implicated in numerous diseases and are designated targets for 50% of pharmaceutical compounds. Members of the Solute Sodium Symporter (SSS) family of proteins carry out the co-transport of Na+ with a diverse group of substrates including sugars, amino acids, inorganic ions or vitamins. There are 12 human members that play critical roles in the physiology of the brain, intestine, kidneys, and thyroid, where mutations in their genes are responsible for severe congenital diseases. Furthermore, human SSS family members are the molecular targets for drugs to treat diabetes, obesity and infectious diarrhea. Therefore, the primary objective of my graduate studies was to solve the crystal structure of sodium galactose symporter from Vibrio parahaemolyticus, bacterial member of SSS family, in order to elucidate the structural basis for co-transport.

ISBN: 9781267753984Subjects--Topical Terms:

518360
Biophysics.

Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus.
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245 1 0 $a Structural and Functional Studies of Sodium Galactose Symporter from Vibrio parahaemolyticus.
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500 $a Source: Dissertation Abstracts International, Volume: 74-03(E), Section: B.
500 $a Adviser: Jeffrey Abramson.
502 $a Thesis (Ph.D.)--University of California, Los Angeles, 2012.
520 $a Secondary active transporters are essential components of physiology in all organisms. They utilize the energy stored in electrochemical gradients of ions to pump specific molecules across the otherwise impermeable membrane bilayer that surrounds all cells and organelles. They are implicated in numerous diseases and are designated targets for 50% of pharmaceutical compounds. Members of the Solute Sodium Symporter (SSS) family of proteins carry out the co-transport of Na+ with a diverse group of substrates including sugars, amino acids, inorganic ions or vitamins. There are 12 human members that play critical roles in the physiology of the brain, intestine, kidneys, and thyroid, where mutations in their genes are responsible for severe congenital diseases. Furthermore, human SSS family members are the molecular targets for drugs to treat diabetes, obesity and infectious diarrhea. Therefore, the primary objective of my graduate studies was to solve the crystal structure of sodium galactose symporter from Vibrio parahaemolyticus, bacterial member of SSS family, in order to elucidate the structural basis for co-transport.
520 $a To achieve this goal, I modified the pre-existed protocol for vSGLT expression and purification to obtain a pure, stable, and homogenous sample of vSGLT. Using this for crystallization as well as identifying detergents more suitable for crystallization, I took several approaches to obtain phase for initial structure and to obtain alternate conformation of vSGLT.
520 $a As a result, I was able to solve crystal structures of vSGLT in inward-occluded conformation with bound substrates and inward-open conformation without substrates. These allowed me to identify substrate and sodium binding sites and common structural core among different membrane transporters. Analysis of these different membrane transporters and combining two vSGLT structures with molecular dynamics simulations revealed the mechanism of substrate release from the binding pocket of vSGLT.
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