Membrane interaction of the N-terminal domain of chemokine receptor CXCR1 |
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Authors: | Sourav Haldar H Raghuraman Trishool Namani Amitabha Chattopadhyay |
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Institution: | a Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Uppal Road, Hyderabad 500 007, India b Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, the University of Texas Medical Branch, Galveston, TX 77555-1055, USA |
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Abstract: | The N-terminal domain of chemokine receptors constitutes one of the two critical ligand binding sites, and plays important roles by mediating binding affinity, receptor selectivity, and regulating function. In this work, we monitored the organization and dynamics of a 34-mer peptide of the CXC chemokine receptor 1 (CXCR1) N-terminal domain and its interaction with membranes by utilizing a combination of fluorescence-based approaches and surface pressure measurements. Our results show that the CXCR1 N-domain 34-mer peptide binds vesicles of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and upon binding, the tryptophan residues of the peptide experience motional restriction and exhibit red edge excitation shift (REES) of 19 nm. These results are further supported by increase in fluorescence anisotropy and mean fluorescence lifetime upon membrane binding. These results constitute one of the first reports demonstrating membrane interaction of the N-terminal domain of CXCR1 and gain relevance in the context of the emerging role of cellular membranes in chemokine signaling. |
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Keywords: | CXCR1 CXC chemokine receptor 1 DMPC 1 2-dimyristoyl-sn-glycero-3-phosphocholine DOPC 1 2-dioleoyl-sn-glycero-3-phosphocholine DPC dodecylphosphocholine GPCR G-protein coupled receptor LUV large unilamellar vesicle MOPS 3-(N-morpholino)propanesulfonic acid REES red edge excitation shift |
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