Protein Structure and Ion Binding in Potassium Selective Channels

Potassium channels play a central role in a number of biological processes, most classically the action potential of excitable cells in multicellular organisms. These channels are defined by their selective conduction of potassium to the exclusion of other monovalent ions as governed by a common sequence and structural motif, the selectivity filter. This structure, made of backbone carbonyls and threonine side chains, directly coordinates the ions as they diffuse through the channel and appears central to this sub-angstrom discrimination between cations. Utilizing the non-selective Sodium and Potassium conducting channel (NaK) as a structural scaffold the mechanisms of both ion selectivity and formation of this selective structure are examined.

Name thesis:degree_name

Doctor of Philosophy

Level thesis:degree_level

Doctoral

Discipline thesis:degree_discipline

Molecular Biophysics

Grantor

UT Southwestern Medical Center

Year dc:date.issued

2013

Author dc:creator

• Sauer, David Bryant

Advisor dc:contributor.advisor

• Jiang, Youxing

• Sodium-Potassium-Exchanging ATPase
• Potassium
• Models, Molecular

Identifier

841563990

OAI record oai:identifier

https://utswmed-ir.tdl.org/server/oai/request?verb=GetRecord&metadataPrefix=dim&identifier=oai%3Autswmed-ir.tdl.org%3A2152.5%2F1262