Structural Similarity of a Membrane Protein in Micelles and Membranes
Sanford-Burnham Medical Research Institute, لا هویا, California, United StatesJournal of the American Chemical Society (Impact Factor: 12.11). 08/2007; 129(26):8078-9. DOI: 10.1021/ja0728371
The anisotropic spin interactions measured for membrane proteins in weakly oriented micelles and in oriented lipid bilayers provide independent and potentially complementary high-resolution restraints for structure determination. Here we show that the membrane protein CHIF adopts a similar structure in lipid micelles and bilayers, allowing the restraints from micelle and bilayer samples to be combined in a complementary fashion to enhance the structural information. Back-calculation and assignment of the NMR spectrum of CHIF in oriented lipid bilayers, from the structure determined in micelles, provides additional restraints for structure determination as well as the global orientation of the protein in the membrane. The combined use of solution and solid-state NMR restraints also affords cross-validation for the structural analysis.
Full-textDOI: · Available from: Peter Teriete, Oct 08, 2015
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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.Current Protein and Peptide Science 10/2012; 13(6):585-600. DOI:10.2174/138920312803582979 · 3.15 Impact Factor
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- "e l s e v i e r . c o m / l o c a t e / b b a m e m experiments have shown that native protein quaternary structure may be maintained in detergent environments  ; aspects of secondary and tertiary structure may be similar in lipid bilayer versus micelle environments ; and the overall fold of a protein may persist in detergents . We have recently observed that the interaction of designed TM segments with detergents is highly sequencedependent , and in many cases mimics the predicted in vivo formation of both helix–helix and protein–lipid interactions  . "
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Human Respiratory Syncytial Virus Infection, 11/2011; , ISBN: 978-953-307-718-5
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