Solid-state NMR and membrane proteins

Opella, Stanley J.

doi:10.1016/j.jmr.2014.11.015

Cited by 29 publications

(23 citation statements)

References 87 publications

(100 reference statements)

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“…Solid-state NMR spectroscopy enables studies of the structure and dynamics of membrane proteins in near-native phospholipid bilayer environments (37)(38)(39)(40). There are several examples where solid-state NMR methods have been used to characterize the structures of ligands bound to GPCRs (41)(42)(43)(44) as well as GPCRs themselves.…”

Section: Introductionmentioning

confidence: 99%

Interaction of Monomeric Interleukin-8 with CXCR1 Mapped by Proton-Detected Fast MAS Solid-State NMR

Park

Berkamp

Radoicic

et al. 2017

Biophysical Journal

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The human chemokine interleukin-8 (IL-8; CXCL8) is a key mediator of innate immune and inflammatory responses. This small, soluble protein triggers a host of biological effects upon binding and activating CXCR1, a G proteincoupled receptor, located in the cell membrane of neutrophils. Here, we describe 1 H-detected magic angle spinning solid-state NMR studies of monomeric IL-8 (1-66) bound to full-length and truncated constructs of CXCR1 in phospholipid bilayers under physiological conditions. Cross-polarization experiments demonstrate that most backbone amide sites of IL-8 (1-66) are immobilized and that their chemical shifts are perturbed upon binding to CXCR1, demonstrating that the dynamics and environments of chemokine residues are affected by interactions with the chemokine receptor. Comparisons of spectra of IL-8 (1-66) bound to full-length CXCR1 (1-350) and to N-terminal truncated construct NT-CXCR1 (39-350) identify specific chemokine residues involved in interactions with binding sites associated with N-terminal residues (binding site-I) and extracellular loop and helical residues (binding site-II) of the receptor. Intermolecular paramagnetic relaxation enhancement broadening of IL-8 (1-66) signals results from interactions of the chemokine with CXCR1 (1-350) containing Mn 2þ chelated to an unnatural amino acid assists in the characterization of the receptor-bound form of the chemokine.

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Section: Introductionmentioning

confidence: 99%

Interaction of Monomeric Interleukin-8 with CXCR1 Mapped by Proton-Detected Fast MAS Solid-State NMR

Park

Berkamp

Radoicic

et al. 2017

Biophysical Journal

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“…It is an honor to follow two friends and colleagues, the late Iain Campbell and Stanley J. Opella, who introduced the NMR perspective in earlier issues of this review series [19,74]. I first met Iain Campbell whilst both of us were postdoctorates in Oxford in 1967.…”

Section: Personal Perspectivementioning

confidence: 99%

The evolution of biomedical EPR (ESR)

Berliner

2017

BSI

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Abstract. Since the first EPR/ESR spectrum of a paramagnetic substance was published over 70 years ago, the technical improvements did not occur until after/during World War II with the advent of radar technology. The approaches to biomedical problems started somewhat later with the real burst of activity starting after the birth of the spin label technique about 50 years ago. The applications to proteins, then membranes and nucleic acids, and later applications to cells and eventually in-vivo on small animals and now humans has led EPR/ESR to finally being recognized as a uniquely powerful technique in the toolbox of techniques probing macromolecules and their interactions, free radical biology and its eventual value as a diagnostic technique. This article gives an overview of EPR/ESR studies of biomedically related systems, including proteins and enzymes. It presents a very personal historical perspective, briefly reviews the origins of the technique and reflects on possible future directions. As with NMR, advances in molecular biology and technology drastically changed the nature and focus of the technique, particularly the site directed spin labeling method that has been invaluable in determining protein and macromolecular structure by both EPR and NMR.

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“…Usually, this type of interaction appears as a dynamically averaged chemical-shift pattern from which orientation constraints for peptides and proteins in a lipid-bilayer environment can be derived. These constraints provide the dynamic structures and orientations of membrane-associated peptides and proteins [9]. Another interaction to be considered as a structural constraint is dipolar interaction between coupled nuclei.…”

Section: Introductionmentioning

confidence: 99%