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
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
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