Abstract
Membrane proteins play important roles in signal transduction across the cell membrane. Structural information for the membrane proteins is still limited due to many technical challenges. Membrane proteins containing a single α- helical transmembrane (TM) domain are very important in several pathways. Solution NMR spectroscopy is an important tool for the study of the structure of the TM domain of these types of proteins due to their small size. In this review, we summarize the importance of some single-span membrane proteins in signal transduction and the importance of understanding the structure of the TM domain. We discussed the current progress in the structural study of these types of proteins using solution NMR spectroscopy. We summarize the structures solved during last several years. The structures of the regulatory domain of the ion channels such as KCNE1, integrin and viral proteins such as the M2 channel are described. The binding interface of single TM-TM domains is discussed based on NMR structural studies. Strategies including sample preparation, detergent screening, and structural determination of single-span membrane protein are summarized. We also discuss the potential application of NMR spectroscopy to drug discovery of proteins with a single-span TM domain.
Keywords: NMR spectroscopy, membrane protein, single-span membrane protein, structure determination, protein-protein interaction, Integral membrane proteins, Genome analysis, KCNQ1, Adhesion molecules, membrane-associated enzyme complex
Current Protein & Peptide Science
Title:Solution NMR Study of the Transmembrane Domain of Single-Span Membrane Proteins: Opportunities and Strategies
Volume: 13 Issue: 6
Author(s): Shovanlal Gayen, Qingxin Li and Congbao Kang
Affiliation:
Keywords: NMR spectroscopy, membrane protein, single-span membrane protein, structure determination, protein-protein interaction, Integral membrane proteins, Genome analysis, KCNQ1, Adhesion molecules, membrane-associated enzyme complex
Abstract: Membrane proteins play important roles in signal transduction across the cell membrane. Structural information for the membrane proteins is still limited due to many technical challenges. Membrane proteins containing a single α- helical transmembrane (TM) domain are very important in several pathways. Solution NMR spectroscopy is an important tool for the study of the structure of the TM domain of these types of proteins due to their small size. In this review, we summarize the importance of some single-span membrane proteins in signal transduction and the importance of understanding the structure of the TM domain. We discussed the current progress in the structural study of these types of proteins using solution NMR spectroscopy. We summarize the structures solved during last several years. The structures of the regulatory domain of the ion channels such as KCNE1, integrin and viral proteins such as the M2 channel are described. The binding interface of single TM-TM domains is discussed based on NMR structural studies. Strategies including sample preparation, detergent screening, and structural determination of single-span membrane protein are summarized. We also discuss the potential application of NMR spectroscopy to drug discovery of proteins with a single-span TM domain.
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Cite this article as:
Gayen Shovanlal, Li Qingxin and Kang Congbao, Solution NMR Study of the Transmembrane Domain of Single-Span Membrane Proteins: Opportunities and Strategies, Current Protein & Peptide Science 2012; 13 (6) . https://dx.doi.org/10.2174/138920312803582979
DOI https://dx.doi.org/10.2174/138920312803582979 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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