Membrane interaction of the N-terminal domain of chemokine receptor CXCR1

Haldar, Sourav ; Raghuraman, H. ; Namani, Trishool ; Rajarathnam, Krishna ; Chattopadhyay, Amitabha (2010) Membrane interaction of the N-terminal domain of chemokine receptor CXCR1 Biochimica et Biophysica Acta (BBA) - Biomembranes, 1798 (6). pp. 1056-1061. ISSN 0005-2736

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00052...

Related URL: http://dx.doi.org/10.1016/j.bbamem.2010.02.029

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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Chemokine Receptor; G-protein Coupled Receptor; Surface Pressure; Red Edge Excitation Shift; Membrane Vesicle; Lipid Monolayer
ID Code:7178
Deposited On:25 Oct 2010 12:20
Last Modified:16 May 2016 17:25

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