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H,C andN resonance assignments for a chemokine receptor-binding domain of FROUNT, a cytoplasmic regulator of chemotaxis.

H,C andN resonance assignments for a chemokine receptor-binding domain of FROUNT, a cytoplasmic regulator of chemotaxis.
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Yoshinaga S, Ishida N, Tsuji T, Sonoda A, Yunoki K, Takeda M, Toda E, Terashima Y, Matsushima K, Terasawa H,


Yoshinaga S, Ishida N, Tsuji T, Sonoda A, Yunoki K, Takeda M, Toda E, Terashima Y, Matsushima K, Terasawa H, (click to view)

Yoshinaga S, Ishida N, Tsuji T, Sonoda A, Yunoki K, Takeda M, Toda E, Terashima Y, Matsushima K, Terasawa H,

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Biomolecular NMR assignments 2018 03 28() doi 10.1007/s12104-018-9819-2

Abstract

FROUNT is a cytoplasmic protein that interacts with the membrane-proximal C-terminal regions (Pro-Cs) of the CCR2 and CCR5 chemokine receptors. The interactions between FROUNT and the chemokine receptors play an important role in the migration of inflammatory immune cells. Therefore, FROUNT is a potential drug target for inflammatory diseases. However, the structural basis of the interactions between FROUNT and the chemokine receptors remains to be elucidated. We previously identified the C-terminal region (residues 532-656) of FROUNT as the structural domain responsible for the Pro-C binding, referred to as the chemokine receptor-binding domain (CRBD), and then constructed its mutant, bearing L538E/P612S mutations, with improved NMR spectral quality, referred to as CRBD_LEPS. We now report the main-chain and side-chainH,C, andN resonance assignments of CRBD_LEPS. The NMR signals of CRBD_LEPS were well dispersed and their intensities were uniform on theH-N HSQC spectrum, and thus almost all of the main-chain and side-chain resonances were assigned. This assignment information provides the foundation for NMR studies of the three-dimensional structure of CRBD_LEPS in solution and its interactions with chemokine receptors.

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