자료유형  

 학위논문

Control Number  

0016934419

International Standard Book Number  

9798380321273

Dewey Decimal Classification Number  

612

Main Entry-Personal Name  

Chew, Thomas Andrew.

Publication, Distribution, etc. (Imprint  

[S.l.] : Stanford University., 2021

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2021

Physical Description  

1 online resource(97 p.)

General Note  

Source: Dissertations Abstracts International, Volume: 85-03, Section: B.

General Note  

Advisor: Kobilka, Brian K.;Maduke, Merritt C.;Feng, Liang.

Dissertation Note  

Thesis (Ph.D.)--Stanford University, 2021.

Restrictions on Access Note  

This item must not be sold to any third party vendors.

Summary, Etc.  

요약Ion transport is fundamental to cell homeostasis, and plays an important role in numerous physiological processes such as cell signaling and volume regulation. The cation-chloride cotransporter (CCC) family of proteins is critical for regulating volume through the careful control of sodium, potassium, and chloride transport. The intricate balance and transport of these diverse ions is responsible for maintaining cellular health, with various diseases arising when dysregulation occurs. Given their importance, CCC family members serve as major drug targets. Such proteins have been studied for decades, but structural information has been lacking due to the difficulty associated with studying membrane proteins of this size, as well as a relatively disordered N-terminus. However, in recent years technical advances in cryo-electron microscopy (cryo-EM) have made it possible to study proteins such as CCC transporters in far greater detail. Here, I describe my efforts to understand the mechanism of action of a particular member of the CCC transporter family, NKCC1. NKCC1 transports sodium, potassium, and chloride in cells throughout the body. I describe the structure of NKCC1, which shows the general fold of the CCC transporter family and the unique positioning of both cytosolic and transmembrane domains. The structure of this protein, combined with functional studies and molecular dynamics simulations allow for a deeper understanding of the CCC family of proteins. Aspects covered include the overall structure of the protein, identification of specific residues responsible for ion binding, and a proposed transport mechanism. Together, these studies shed light on this important family of proteins.

Subject Added Entry-Topical Term  

Physiology.

Subject Added Entry-Topical Term  

Phylogenetics.

Subject Added Entry-Topical Term  

Mutation.

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Binding sites.

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Data processing.

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Infrared imaging systems.

Subject Added Entry-Topical Term  

Chromatography.

Subject Added Entry-Topical Term  

Potassium.

Subject Added Entry-Topical Term  

Lipids.

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Drug dosages.

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Signal transduction.

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Cells.

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Adenosine triphosphatase.

Subject Added Entry-Topical Term  

Diuretics.

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Blood pressure.

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Sodium.

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Sensors.

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Hypertension.

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Microscopy.

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Genetics.

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Medicine.

Subject Added Entry-Topical Term  

Systematic biology.

Added Entry-Corporate Name  

Stanford University.

Host Item Entry  

Dissertations Abstracts International. 85-03B.

Host Item Entry  

Dissertation Abstract International

Electronic Location and Access  

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Control Number  

joongbu:642069